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Hemolysis in glucose-6-phosphate dehydrogenase (G6PD) deficiency varies by mutation status and the oxidative stressor. Although classified by percent of enzymatic deficiency, variability in normal G6PD values clouds assessment of hemolysis risk by level. This was a retrospective, single institution, cohort study assessing risk of postexposure medication-induced hemolysis in G6PD deficient patients. Exposures occurred in 87 of 1415 deficient patients. Only 2 of 87 medication-exposed patients had hemolytic episodes and both had very low enzymatic activity. No hemolytic events occurred with G6PD levels >7 units/g hemoglobin. Correlation of levels with mutation may improve predictive capacity for hemolysis in G6PD deficiency.

In modern aviation, so-called fume events such as exposure to an unknown mixture of chemicals introduced into the aircraft cabin with bleed air drawn off at the engines may occur. Human exposure may result in (neuro)toxic symptoms described as so-called "aerotoxic syndrome." Currently, among other agents organophosphates (OP) are regarded as a likely cause of the observed adverse effects. After fume events 11 flight crew members (9 female/2 male; ages 23-58 yr) were admitted for a medical examination within 5 d post exposure. Individual acetylcholinesterase (AChE) and neuropathy target esterase (NTE) activities were determined. Anamnesis and clinical findings confirmed prominent symptoms of an intoxication, including headache, cognitive difficulties, and neurological disorders, among others. Patient AChE activities ranged from 37 to 50 U/g hemoglobin (reference values: 26.7-50.9 U/g hemoglobin). Ten individuals showed NTE activities ranging from 3.14 to 6.3 nmol phenyl valerate/(min × mg protein) (reference values: 3.01-24), with one patient exhibiting low NTE activity of 1.4. Biochemical effect monitoring was applied to encompass a broad range of AChE-inhibiting compounds such as OP, carbamates, and isocyanates, or to detect inhibition of NTE. The measured AChE activities indicated a subordinate contribution of OP or related compounds to the observed symptoms. All noted NTE activities were clustered at low levels. Our data suggest a likely inhibition of NTE activities in patients after fume events, which warrants further investigation. The observed symptoms may be linked to known chemical compounds in fume events, and it is not possible to infer a direct correlation between manifestations and AChE -inhibiting compounds at this time.

BACKGROUND Each unit of blood donated is processed and stored individually resulting in variability in the amount of red blood cells (RBCs) collected, RBC properties, and the 24-hour posttransfusion RBC survivability. As a result, each unit differs in its ability to deliver oxygen and potentially its effects on the recipient. The goal of this study was to investigate the storage of pooled RBCs from multiple donors in comparison to control standard RBC units. STUDY DESIGN AND METHODS Two units of irradiated, leukoreduced RBCs of same ABO, D, E, C, and K antigen phenotype were collected from each of five donors using apheresis. One unit from each donor was pooled in a 2-L bag and remaining units were used as controls. After being pooled, RBCs were separated in five bags and stored at 4°C along with the controls. Quality indexes were measured on Days 2, 14, and 28 for all the units. RESULTS Adenosine triphosphate assays for both pooled and controls showed a slight decrease from Day 2 to Day 28 (pooled/control from 5.22/5.24 to 4.35/4.33 µmol/g hemoglobin [Hb]). 2,3-Diphosphoglycerate was successfully rejuvenated for all RBC units on Day 28 (pooled 11.46 µmol/g Hb; control 11.86 µmol/g Hb). The results showed a nonsignificant difference between pooled and control units, with a general trend of lower standard deviation for pooled units when compared to controls. CONCLUSION Pooled units have reduced unit-to-unit variability. Future exploration of their immunogenicity is required before using pooled units for transfusion.

We report a clinical update of the hemoglobin (Hb) variant [β27(B9)Ala→Gly; HBB: c.83C>G], named Hb Siirt, that was previously described as a silent variant in a 23-year-old Kurdish female. The patient was also a carrier of the codon 5 (–CT) (HBB: c.17_18delCT) frameshift mutation and of the ααα anti 3.7 triplication. Her initial moderate β-thalassemia intermedia (β-TI) phenotype worsened with time, causing the patient to become a transfusion-dependent subject at the age of ∼40 years. Subsequent molecular characterization of both parents revealed that the Hb Siirt variant was inherited by the mother, while the other two globin alterations (HBB: c.17_18delCT and αααanti 3.7 triplication) were genetically transmitted by the father. The latter remained a carrier of a mild β-TI phenotype throughout his life, at least until the age of 65 years. We hypothesize that the worsened clinical conditions in the daughter were due to the additional, maternally inherited Hb Siirt variant. However, protein 3D conf...

Glucose-6-Phosphate dehydrogenase (G6PD) is an enzyme present in the cytoplasm of all cells in the body and protects red blood cells from certain attacks. The anomaly is genetically inherited in a recessive manner, linked to the X chromosome. Currently, an estimated 420 million individuals lack G6PD worldwide and its incidence varies between 1-25% in some African populations. This was an analytical cross-sectional study with prospective data collection that took place from May to November 2018, i.e. six (6) months. Our study included 108 blood donors, 88 men and 20 women. The samples were stored at 2-8 ° C for 24 hours while awaiting handling. The determination of the enzymatic activity of G6PD was carried out by the spectrophotometric method using a commercially available kit. 02/108 subjects studied (ie a prevalence of 1.85%) were deficient in our study. These two deficit were mostly young and between 18-25 years old only male. They were originally from the plateau and observed in the blood transfusion station (PTS) of the Talangai referral hospital. The mean hemoglobin value in normal subjects was 12.53 g / dl in men and 11.3 g / dl in women. In contrast, the average hemoglobin value was 10.45 g / dl in the deficient patients. The mean value of G6PD enzyme activity in normal subjects was 11.7 IU / g hemoglobin in men, 11.54 IU / g hemoglobin in women and in deficient subjects was 2.83 IU / g hemoglobin. As the results of our study show, G6PD deficiency affects hemoglobin levels.

Accurate diagnosis of glucose-6-phosphate dehydrogenase (G6PD) deficiency is required to avoid the risk of acute hemolysis associated with 8-aminoquinoline treatment. The performance of the BinaxNOW G6PD test compared with the quantitative spectrophotometric analysis of G6PD activity was assessed in 356 Plasmodium vivax-infected subjects in Brazil, Peru, Thailand, and India. In the quantitative assay, the median G6PD activity was 8.81 U/g hemoglobin (range = 0.05-20.19), with 11 (3%) subjects identified as deficient. Sensitivity of the BinaxNOW G6PD to detect deficient subjects was 54.5% (6 of 11), and specificity was 100% (345 of 345). Room temperatures inadvertently falling outside the range required to perform the rapid test (18-25 degrees C) together with subtlety of color change and insufficient training could partially explain the low sensitivity found. Ensuring safe use of 8-aminoquinolines depends on additional development of simple, highly sensitive G6PD deficiency diagnostic tests suitable for routine use in malaria-endemic areas.

BACKGROUND: Red blood cells (RBCs) are Food and Drug Administration (FDA)-approved for 42-day storage with the use of additive solutions (ASs). However, adenosine triphosphate (ATP) and 2,3-diphosphoglycerate (2,3-DPG) levels in the RBCs decline over this time. These constituents may be restored by treatment with rejuvenation (REJ) solutions. This study was done to assess the response capability of RBCs from 30 to 120 days of storage in three FDA-licensed RBC storage solutions after incubation with a rejuvenating solution of pyruvate, inosine, phosphate, and adenine. STUDY DESIGN AND METHODS: Three units each of RBCs in approved AS (AS-1 [Adsol, Fenwal, Inc.], AS-3 [Nutricel, Medsep Corp.], and AS-5 [Optisol, Terumo Corp.]) were stored under standard conditions at 1 to 6°C for up to 120 days. Aliquots (4 mL) on Days 30, 42, 60, 80, 100, and 120 (±2 days) were REJ by incubating with Rejuvesol (Encyte Corp.). Control untreated and REJ aliquots were extracted using perchloric acid and stored at −80°C until assayed for 2,3-DPG and ATP. RESULTS: RBCs responded to REJ by increasing DPG and ATP contents. The response declined linearly at 0.070 ± 0.008 µmol DPG/g hemoglobin (Hb)/day and 0.035 ± 0.004 µmol ATP/g Hb/day with no differences between ASs. CONCLUSION: We conclude that Rejuvesol is able to restore ATP and 2,3-DPG levels in RBCs stored up to 120 days in AS. The response diminishes as storage time increases. This rejuvenation (REJ) capability does not seem useful for routine assessment of RBC anabolic capacity in research programs, but may be useful to the investigator when studying unique and novel treatment methods.

BACKGROUND: Whole blood (WB) can be stored overnight before processing, provided that it is quickly cooled to room temperature (20-25°C), for example, with butane-1,4-diol plates. A new design of cooling plates became available (CompoCool-WB, Fresenius HemoCare), where WB must be placed vertically against the plates, versus placing of WB under plates in the current version (Compocool). This study compared cooling efficiency and in vitro quality of plasma and of stored white cell (WBC)-reduced red cells (RBCs) from overnight-stored WB, cooled with either of the systems. STUDY DESIGN AND METHODS: Temperature curves following cooling with Compocool or CompoCool-WB were studied with a 25 percent glycerol solution as simulated WB. WB from voluntary donors was cooled with Compocool or CompoCool-WB, stored overnight at room temperature, centrifuged, and separated into components. WBC-reduced RBCs in SAGM were stored until Day 42 with measurement of in vitro parameters (n = 23/group). RESULTS: Simulated WB reached a temperature of less than 25°C after 2:15 ± 1:04 hours for Compocool versus 1:39 ± 0:38 hours for CompoCool-WB (p = 0.02). On Day 35, RBCs had a hemolysis of 0.3 ± 0.2 percent in both groups, and ATP levels were 3.3 ± 0.5 and 3.6 ± 0.5 µmol per g hemoglobin for Compocool and CompoCool-WB, respectively (not significant). Factor VIII content in plasma was 1.05 ± 0.25 and 0.97 ± 0.18 IU per mL for Compocool and CompoCool-WB, respectively. CONCLUSION: WB can be cooled to room temperature within 2 hours with both Compocool and CompoCool-WB butane-1,4-diol plates, improving temperature uniformity in WB donations. Application of either design for overnight storage of WB at room temperature had no adverse effects on the composition of subsequently prepared blood components.

Equine carbonic anhydrase isozymes (CA-I and CA-II) were purified from erythrocytes by several column chromatography. Polyclonal anti-CA-I and anti-CA-II sera were produced in rabbits. Sensitive competitive enzyme-linked immunosorbent assays (ELISA) were established to determine the developmental changes in CA-I and CA-II levels in equine erythrocytes. Concentrations of CA-I and CA-II in erythrocytes from 150 clinically normal thoroughbreds (123 racehorses and 27 riding horses) were determined by ELISA. Mean (+/- SD) concentrations of CA-I and CA-II in racehorses were 1.70 +/- 0.48 and 0.94 +/- 0.13 mg/g hemoglobin (Hb), respectively. Mean concentrations of CA-I and CA-II in riding horses were 2.34 +/- 0.52 and 0.76 +/- 0.08 mg/g Hb, respectively. When the CA levels in racehorses and riding horses were compared, the CA-I level in riding horses was higher than that in racehorses (p=0.01). The CA-II level in racehorses was higher than that in riding horses (p=0.02). These data suggest that the levels of CA isozymes in erythrocytes of racehorses were influenced by chronic physical stress. The CA-I concentration in erythrocytes of 2-month-old horses was approximately 0.25 mg/g Hb. The CA-I level noticeably increased during the first year of life and approached normal adult levels by 2 years. The CA-II level decreased slightly with age, indicating different regulation of CA-I and CA-II expression during development.

An additive solution for the storage of red blood cells was evaluated for use in dogs. Blood collected from 6 dogs was processed into packed red blood cells and stored for 35 days in the additive solution Nutricel (Miles, Inc, Pharmaceutical Division, West Haven, CT). Packed red blood cells stored in citrate-phosphate-dextrose-adenine (CPDA-1; Fenwal Laboratories, Baxter Health Care Corp, Deerfield, IL) also were evaluated for comparison. Red blood cell 2,3-diphosphoglycerate (2,3-DPG) concentration, adenosine triphosphate (ATP) concentration, percentage hemolysis, and pH were determined. The red blood cell post-transfusion viability (PTV) after 35 days of storage was assessed with both single-labeled chromium 51 (51Cr) and double-labeled technetium 99m/chromium 51 (99mTc/51Cr) techniques. Mean ATP concentration and percentage hemolysis of the cells stored in Nutricel were 1.1 mumol/g hemoglobin (Hb) and 0.28% respectively and did not differ significantly (P < .05) from the values of 1.0 mumol/g Hb and 0.33% from the CPDA.1-stored red blood cells. The mean pH of red blood cells stored in Nutricel was 6.19, which was significantly lower than the pH of 6.47 for cells stored in CPDA-1. The mean 2,3-DPG concentration of red blood cells stored in Nutricel was significantly higher at 10.1 mumol/g Hb than the 2,3-DPG concentration of 3.4 mumol/g Hb for cells stored in CPDA-1. The mean PTV of canine red blood cells stored in Nutricel for 35 days was 85% with 51Cr and 90% with 99mTc/51Cr. This was significantly higher than the mean PTVs of 38% and 36% for the CPDA-1 stored cells as assessed with 51Cr and 99mTc/51Cr techniques, respectively. It was concluded that 35-day-old canine red blood cells stored in Nutricel are of acceptable quality for transfusion purposes.

Aim: Our purpose was to determine the frequency of glucose-6-phosphate dehydrogenase (G6PD) deficiency in blood donors of Jahrom, Iran. Methods: Blood samples were obtained from the 706 blood donors who referred to Jahrom Blood Transfusion Organization between June and September 2008. Enzyme assays were performed three times, on day 1 (day of blood sampling), 7 and 45 days after blood storage. G6PD activity was measured using a quantitative assay. Results: A total of 706 samples were examined. 97.7% males and 2.3% females, mean age 32.6 years (18–64 years). Based on enzyme activity less than 1.62 IU/g hemoglobin (Hb), prevalence of G6PD deficiency in three separate measurements was 16.3, 19.1 and 33.3% respectively. Four percent of donor had an enzyme level of zero on day 1 which increased to 7.4 and 10.7% on the seventh and the forty-fifth days. Conclusion: The results of this study support the screening for G6PD as part of the routine workup of blood donors in areas with a high prevalence of G6PD deficiency.

Abstract 3437 Each unit of blood donated is processed and stored individually resulting in wide variability in the amount of red blood cells (RBCs) collected, RBC properties and in the 24 hour post-transfusion RBC survivability. As a result, each unit differs in its RBC content, its ability to deliver oxygen and potentially its effects on the recipient. The goal of this study was to investigate the effect of pooling and the use of novel additive solutions in producing a more uniform, standardized RBC product. RBCs were either stored in an approved additive solution with a 42 day shelf life (AS-3) or a solution which potentially enables an extended 50 to 100 day shelf life (EAS-81). The storage characteristics of individual RBC units were compared to pooled RBC products prepared by the same units and suspended in AS-3 and EAS-81 with comparable final hematocrits. Two sets of 5 individual leukoreduced group A, D-positive blood group RBC units were divided and stored as individual RBC products or as pooled products. Individual and pooled units tested as group A, D-positive and had a negative antibody screen. Quality indices were measured (ATP, 2,3 DPG and hemolysis) for all individual and pooled units weekly for 5 weeks. After 5 weeks of storage RBC units stored in EAS-81 showed higher ATP concentrations (2.53–4.20 μmole/g hemoglobin) compared to units stored in AS-3 solution (1.53–1.98 μmole/g hemoglobin). ATP concentration values of pooled units of EAS81:AS-3 (3.35:1.77 μmole/g hemoglobin) were close to average (3.24:1.64 μmole/g hemoglobin) values obtained from 5 individual unit concentrations (Figure). Next, after 5 weeks hemolysis was higher in EAS-81 (0.57–0.94% hemolysis) as compared to AS-3 solution (0.18–0.35% hemolysis); possibly due to cells being passed through an additional leukoreduction filter. The hemolysis values of pooled units of EAS-81: AS-3 (0.51:0.27%) was lower for EAS-81 but the same for AS-3 as the average values obtained from individual units (0.80:0.27%). Lastly, after 2 weeks of storage 2,3 DPG values obtained were lower for AS-3 units (2.71–3.84 μmole/g hemoglobin) as compared to EAS-81 units (3.40–7.10 μmole/g hemoglobin). 2,3-DPG concentration of pooled unit EAS-81:AS-3 (7.10:3.38 μmole/g hemoglobin) were higher compared to average of individual unit (4.74:3.19 μmole/g hemoglobin). 2,3 DPG concentration was negligible for 3 week measurement for all the units. In conclusion, RBCs stored in EAS-81 have higher ATP and 2,3-DPG levels than units stored in AS-3; pooled units maintain ABO/D typing without new antibody or antigen formation, and appear to have slightly better storage characteristics than individually stored units. Thus, our data support pooling RBC units is a valid method to provide more uniform RBC products with better storage characteristics, especially if stored in EAS-81, in the future. Disclosures: Stassinopoulos: Cerus: Employment, Equity Ownership, Patents & Royalties. Hess:U. S. Army, Hemerus Medical, LLC: Membership on an entity's Board of Directors or advisory committees, Patents & Royalties.

We determined erythrocyte nucleotides levels in 22 lead workers with blood lead ranging from 8 to 78 micrograms/dl. Their erythrocyte pyrimidine 5'-nucleotidase (P5N) activity ranged from 19.4 to 3.4 mumol uridine/h per g hemoglobin. A significant elevation of erythrocyte pyrimidine nucleotides was found, and their contents correlated inversely with erythrocyte P5N activity and positively with blood lead concentration. In particular, the contents of uridine triphosphate (UTP) and cytidine triphosphate (CTP) exhibited a high correlation with P5N activity (r = -0.56, -0.54). However, its concentration in lead workers was estimated to be much lower than that in hereditary P5N deficiency.

The relationship between the blood NAD and NADP levels and the niacin equivalent intake was investigated using women students. The daily niacin equivalent intake was 151±64μmol (18.5±7.5mg in terms of nicotinamide, mean±SD). The blood NAD and NADP levels were 34.7±7.0 and 19.3±2.3nmol/ml whole blood, respectively. The blood NAD level was proportional to the blood NADP level. Both blood levels were also proportional to the hemoglobin content, and the NAD and NADP levels per g hemoglobin were 233.7±44.7 and 156.3±25.5nmol. The blood NAD and NADP levels increased with an increase in the niacin equivalent intake. From these results, it is concluded that the blood total pyridine nucleotide level (NAD+NADP) reflects the niacin equivalent intake. Accordingly, the blood pyridine nucleotide level may be useful as an index for niacin nutrition in humans.

Pronghorn ( ilocapra americana are probably the second fastest land mammal with a top speed of about 100 km/hr. Pronghorn are endurance runners as well as they have been observed running at an average speed of 65 km/hr for over 10 min. To determine if the pronghorn has become physiologically adapted for running a number of parameters which are thought to influence the delivery of 0 2 uscle and the removal of respiratory and metabolic acids both in the pronghorn and in its unspecialized control, the domestic goat, were measured. Average values obtained are as follows: Pronghorn Goat Heart wt/body wt 0.948 0.495 g/100 g Hemoglobin 18.8 11.5 g/100 ml Blood volume 9.29 6.59% body wt Hematocrit 0.44 0.31 Airway resistance 1.34 2.85 cm H 2 O/L/sec Blood buffering 0.43 0.55 pH drop It is concluded that the pronghorn is physiologically adapted for running compared to goats of equal size.

Fingernail samples from 32 patients with diabetes mellitus and from 26 non-diabetics were analyzed in order to determine the protein glycosylation rate in nail. Nail glycosylation was assayed by the thiobarbituric acid reaction. Blood was taken from both diabetics and non-diabetics at the same time for measurement of hemoglobin glycosylation. In non-diabetics, the protein glycosylation in nail and glycosylated hemoglobin were found to be 8.35 +/- 2.7 nmol fructosamine/mg nail and 2.24 +/- 0.45 mumol fructosamine/g hemoglobin, respectively. In diabetics, however, there was an extremely high glycosylation in both nail protein and hemoglobin: 16.0 +/- 7.35 nmol fructosamine/mg nail and 5.17 +/- 1.17 mumol fructosamine/g hemoglobin (p less than 0.001 for both). A significant correlation was found between nail glycosylation and glycosylated hemoglobin in diabetics (r = 0.923, p less than 0.001). Also, there was a correlation between diabetic fasting blood glucose and protein glycosylation in nail (r = 0.947, p less than 0.001). Our findings show that it might be useful in the investigation of microvascular complications of diabetes mellitus to evaluate the possibility of nail glycosylation providing a stable long-term measure of tissue glycosylation.

Thirty C57BI mice were randomized into two groups. Group 1 served as controls while Group 2 was given 10% V/V ethanol with the drinking water. Whole blood- associated acetaldehyde (WBAA) was measured on capillary blood samples using a fluorigenic high performance chromatographic assay. WBAA peaked at Day 2. A stable mean plateau of 263 +/- 71 SD with a range of 160-400 nmoles/g hemoglobin WBAA was found in the group consuming ethanol compared with 122 +/- 17 SD and a range of 88-150 nmoles/g hemoglobin for controls (p less than 0.001). When ethanol was discontinued, levels of WBAA declined and became similar to those of controls by 9 days following cessation of ethanol. The quantitative difference between ethanol-consuming and control animals and also the rapid rise of whole blood-associated acetaldehyde and the relatively slow decline following cessation of ethanol intake indicate that such a test might be a useful monitor of drinking behavior.

A sensitive and reproducible method for quantitation of polyamines in erythrocytes by high-performance liquid chromatography (HPLC) is described. Spermidine and spermine are first converted to fluorescent dansyl derivatives and are then separated in less than 15 minutes on a C18 reverse-phase cartridge using methanol in water mobile phase. Sensitivity of the method is 20 pmol with recoveries that average 96% and 95% for spermidine and spermine, respectively. Precision study revealed an average mean coefficient of variation of 5.42 ± 2.95 (mean ± S.D.) from four levels of the polyamines (8.2 to 354.9 nmol/g hemoglobin [Hgb]). The normal ranges for 30 apparently healthy men and women, aged 20–60 years, were 2.9–33.7 nmol/g Hgb (± 2 S.D. from mean) for spermidine and 0-20.9 nmol/g Hgb for spermine. The quantity of putrescine was negligible. Feasibility of this method was evaluated in serial specimens from an advanced-stage patient with prostate cancer who was receiving multiple-modality therapy. Results revealed that this HPLC method can be used in quantifying circulating polyamines in clinical specimens.

The selenium status of 13 adult home parenteral nutrition (HPN) patients was evaluated using 12 healthy adult volunteers as controls. Patients had been maintained on HPN for a mean of 36 months and averaged 121 cm of residual small bowel. Prospective diet surveys in patients indicated a mean oral caloric intake of 902 kcal/day. The mean plasma selenium concentrations (microgram/g) were 0.044 in patients and 0.117 in controls (p less than 0.01). The erythrocyte glutathione peroxidase activities, as mumol of NADPH oxidized/g hemoglobin/min, averaged 11.01 in patients and 31.76 in controls (p less than 0.01). Four patients exhibited myalgic symptomatology suggestive of clinical selenium deficiency. No correlations could be ascertained between plasma selenium levels and glutathione peroxidase activities in either patients or controls. Additionally, in the patient group, no significant correlations could be ascertained between selenium status and oral caloric intake, residual small bowel length, symptomatology suggestive of deficiency or HPN duration. However, since sample size was not large, lack of correlations might best be considered suggestive not conclusive. The data indicate that HPN patients with small bowel resections exhibit suboptimal selenium status and may be at risk of developing clinically evident selenium deficiency. HPN patients should be prophylactically supplemented with selenium regardless of oral intake, duration of HPN, or residual length of resected small bowel.

Extract: We have found a genetic trait of arginase deficiency in erythrocytes (RBC) of Macaca fascicularis (crabeater macaque). Measurements of arginase activities and arginine concentrations in RBC, and information derived from breeding experiments indicated that arginase activities in RBC are 12.59 mmoles/g hemoglobin (Hb)/hr (range: 8.36–15.24) in normal monkeys, 4.40 mmoles/g Hb/hr (sd ± 2.37) in hetero-zygotes for this trait, and less than 0.05 mmoles/g Hb/hr in homozygotes for this trait. Concentrations of arginine in erythrocytes are less than 0.01 $mUmoles/ml packed cells in both normal and heterozygous monkeys, and 0.975 $mUmoles/ml packed cells (sd ± 0.556) in homozygous monkeys. There are no significant differences in plasma amino acids and hepatic arginase activity in any animal. Speculation: Study of arginase activity in RBC will be expanded to include a large number of monkeys in order to determine the incidence of arginase deficiency in RBC in this species. The possibility of using these monkeys as an animal model for study of human disease arginase deficiency (e.g., genetic engineering) will be explored.

A modification is described of the automated determination of 2,3-diphosphoglycerate (DPG) in blood [Grisolia, S., et al., Anal. Biochem. 31, 235 (1969)]. Modifications in the manifold result in a sensitive, noise-free, rapid system and the modifications in the preparations of the reagents ensure stability of the diluted standards and blood samples for at least three weeks. Samples are run at the rate of 60/h and sample size can be as small as 5 µl of whole blood. The coefficient of variation of the overall determination of automated DPG and manual hemoglobin is 3.6% and the SD is ±0.77 µmol/g Hb. The normal range is 14.6 ± 2.2 (SD) µmol/g hemoglobin.

In 23 patients with anemia or polycythemia but normal lung function, a statistically significant correlation between hemoglobin concentration in the blood -and the diffusing capacity of the lung for CO was found. A change of 1 g hemoglobin per 100 ml blood changes blood the diffusing capacity for about 6.5 % of the predicted value. The diffusing capacity of the lung membrane will be less than 50 % of the total lung capacity with decreasing hemoglobin concentration in the blood. This result confirms the theory of Koyama and Mochizuki [1969] that the resistance to diffusion of the lung membrane is a function of the hemoglobin concentration of the lung capillary blood.

Plasma selenium concentration and glutathione peroxidase activity in red blood cells were determined in subjects from different age groups. The selenium level (mean +/- SD) found in infancy (0 to 6 months) was 2 +/- 0.6 micrograms/dl, with the lowest value of 1 microgram/dl observed in a 4-month-old infant. These levels were significantly lower (p less than 0.001) than the value of 9.5 +/- 1.1 micrograms/dl found in the adult group and 7.7 +/- 1.3 micrograms/dl found in the group of older children (2 to 15 yr). Younger children (6 to 24 months of age) had intermediate levels of 5 +/- 1.2 micrograms/dl. When the data were plotted on a logarithmic scale as a function of age, the figure shows clearly that the plasma selenium levels increase steadily with age throughout life after an initial drop at 60 to 90 days. There was a satisfactory correlation between the plasma selenium concentration and the enzyme glutathione peroxidase activity in the red blood cells (Spearman's p = 0.45, p less than 0.005). Although very low selenium values were observed, the enzyme glutathione peroxidase activity remained above 10 U/g hemoglobin (with only one exception) in all patients.

Male and female mice were exposed to a simulated altitude of 5,500m for 10, 30 or 90 days. After exposure to altitude for 90 days one group of each sex was then returned to sea level pressures for 10 days. In addition to the expected increases in hematocrit and hemoglobin, altitude exposure increased the 2,3-DPG content of red cells. Maximum values of 2,3-DPG (μmoles/g hemoglobin) occurred after 10 days at altitude and thereafter declined to values comparable to those in sea level mice despite continued exposure to hypoxia.

Abnormal zinc metabolism in a 6-year-old male patient with Landau-Kleffner syndrome (acquired aphasia and convulsive disorder) is the subject of our report. We describe a significant decrease of erythrocyte and plasma zinc levels in the patient as compared with normal. Red blood cell zinc content is normally 38.5 ± 2.7 μg/g hemoglobin v 16.5 μg/g hemoglobin found in the patient. Plasma zinc level is 94.6 ± 10.4 μg/dL in normal in comparison with 50.4 μg/dL in the patient. Normal oral zinc tolerance test performed on the patient precludes altered zinc absorption or increased urinary loss. The possible connection between abnormal zinc metabolism and the pathophysiology of Landau-Kleffner syndrome is discussed. ( J Child Neurol 1987;2:28-30).

The ELISA technique was used to assay carbonic anhydrase I (HCAI) in hemolysates prepared by the elution of dried blood samples from Guthrie cards. The ratio HCAI (mg)/hemoglobin (g) measured in blood samples eluted from Guthrie cards was not significantly different from that determined in aliquots of the same blood samples after storage as erythrocyte (RBC) lysates at -20 degrees C, provided that the dried blood was eluted within three weeks of collection. The normal neonatal mean (SD) RBC HCAI concentrations were 2.05 (1.01) and 1.82 (0.86) mg HCAI/g hemoglobin for females and males respectively. Erythrocyte HCAI concentrations gradually rose with age, approaching normal adult levels by 16 years. Blood from hypothyroid neonates and hypothyroid infants on treatment gave normal HCAI/hemoglobin ratios.

1. 1. Activities of S-adenosylhomocysteine (AdoHcy) hydrolase were measured in tissues of horses with severe combined immunodeficiency. No decrease in activity of the enzyme was detected. 2. 2. The activity in erythrocytes was 14.2 ± 9.2 nmol AdoHcy formed/min/g hemoglobin and in fibroblasts it was 28.0 ± 7.9 nmol AdoHcy formed/min/108 cells. 3. 3. Km values were obtained for hemolysates (0.77 μM) and for fibroblast lysates (0.59 μM). 4. 4. Effects of 2′-deoxyadenosine on enzyme inactivation were studied.

1. Reduced glutathione regeneration rates as measured in erythrocytes of ten horses were considerably lower than rates reported in human and sheep erythrocytes. 2. The activity of enzymes involved in reduced glutathione regeneration was at least three times the observed reduction rate. 3. Despite high glucose-6-phosphate dehydrogenase activity, equine erythrocytes could not adequately accelerate the hexose monophosphate pathway. 4. Activities of enzymes involved in regulating the glycolytic pathway were less than 5 μmoles/min per g hemoglobin; of other glycolytic enzymes greater than 10 μmoles/min per g hemoglobin.

The effect of temperature on the CO 2 transport in the blood of some elasmobranchs ( Scyliorhinus, Mustelus, Torpedo ) was studied in the range of 9 to 25°C and at CO 2 tensions from 2 to 10 torr. The relative change in total CO 2 of whole blood was 2.5% per °C and that of the chemically bound CO 2 in true plasma4 % per °C. The log P CO 2 -pH lines shifted to a lower pH when the temperature was increased. The buffer capacity of true plasma was 10 meq/1 and per pH unit and that of separated plasma 4.2 meq/1 and per pH unit. These values were not affected by temperature. The buffer capacity of 1 g hemoglobin was 0.19 meq/1 pH unit. The molal heat of ionization was 7700 cal/mol. Human blood diluted to the same red cell volume displayed the same relationships between P CO 2 , C CO 2 and pH as dogfish blood. It is concluded that most of the CO 2 transport differences between man and dogfish are due to the lower concentration of the buffer proteins in dogfish rather than to different specific properties of the hemoglobin in dogfish and man.

Plasma and erythrocyte lipid peroxidation levels of 20 patients with histopathologically confirmed testis cancer and 20 healthy control individuals were studied between November 1995 and June 1997. The group with testis cancer had a mean age of 24.8+/-8.2 yr and the control group's mean age was 28.3+/-6.9 yr. Stage distribution of the testis cancer cases were 4 of stage A, 10 of stage B, and 6 of stage C. Blood samples of the patients were drawn after orchiectomy and after 12 h fasting before chemotherapy. Mean plasma and erythrocyte lipid peroxidation levels were detected to be 14.51+/-5.30 nmol malondialdehide (MDA)/mL and 9.30+/-2.06 nmol MDA/g hemoglobin (Hb), respectively, in the testis cancer group, whereas the healthy control group had mean plasma and erythrocyte lipid peroxidation levels of 10.7+/-1.82 nmol MDA/mL and 6.18+/-1.68 nmol MDA/g Hb, respectively. Plasma and erythrocyte lipid peroxidation values of the testis cancer patients were determined to be statistically significantly higher than that of the health control group (p < 0.001, p < 0.001). No significant correlation was determined between plasma, erythrocyte lipid peroxidation levels and tumor markers. In conclusion, it can be said that an increase in the lipid peroxidation may play a role in the pathogenesis of testis carcinomas in addition to the other causes.

OBJECTIVES. We conducted a clinic-based study of erythrocyte cholinesterase levels, pesticide exposures, and health effects among farmworkers and nonfarmworkers to determine risks for exposure and associated morbidity. METHODS. Two hundred two farmworkers and 42 nonfarmworkers were recruited sequentially at two community health centers. Erythrocyte cholinesterase levels were measured colorimetrically. Questionnaires obtained data on demographics, occupational history, exposures, and symptoms. RESULTS. Cholinesterase levels were significantly lower among farmworkers (30.28 U/g hemoglobin) than among nonfarmworkers (32.3 U/g hemoglobin). Twelve percent of farmworkers, but no nonfarmworkers, had very low levels. Farmworkers applying pesticides also had lower cholinesterase levels. One half of farmworkers reported being sprayed by pesticides and working in fields with an obvious chemical smell. Of reported symptoms, only diarrhea was associated with cholinesterase levels. Reported exposures, however, were strongly associated with symptoms. CONCLUSIONS. Farmworkers reported many pesticide exposures that violate state and federal regulations. Farmworkers had cholinesterase levels significantly lower than those of nonfarmworkers, although only spraying pesticides was associated with very low levels.

The deficiency was first found by Ogasawara et al /BBRC 1984, 122, 1344 - 1349, Hum.Genet. 1987, 75, 15 - 18/ to occur in Japan, Seoul and Taipei as one heterozygote in about 30 of the population. In order to find the frequency of the defect in the european area, 410 blood samples have been collected from the blood donors in the county blood center in Gdansk /Poland/. The mean AMP deaminase activity in the erythrocytes was found to be 8.3 μmole ammonia/min per g hemoglobin, which is about 30% less than found in Japan but exactly the same which was found in U.S.A. by Campbell et al. /Clin.Chim Acta 1977, 79, 379 - 385/. Among the 410 individuals investigated 26 displayed half or less of the mean erythrocyte AMP deaminase activity. This could mean that the frequency of the mutant gene is one heterozygote in about 16 of the population in Poland. One case of a complete deficiency of the erythrocyte AMP deaminase activity was found in the family member of one of the heterozygotes. All the deficient subjects appeared to be perfectly healthy, there were no evidence of either anaemia or hemolysis.

Peroxide-induced erythrocyte malonyldialdehyde formation (RBC-MDA) has been used as a measure of polyunsaturated fat autooxidation, a process believed to alter membrane transport and enzyme function. Evidence for this process was sought in erythrocytes of RS patients using the method of Bidder (Life Sciences 30:1021, 1980). For 7 children with stage II-IV RS, RBC-MDA was 432 ± 36 nmoles/g hemoglobin on admission, 323 ± 25 at the nadir, and 478 ± 67 1-4 months after RS. Nadir values differed significantly from admission and from values for 7 siblings(431 ± 28), 5 pediatric intensive care unit (ICU) patients(517 ± 32)and 5 adults (530 ± 40). Corresponding values for plasma vitamin E in RS patients were 556 ± 37 mcg/dl at admission, 473±36 at the nadir, and 905±30 after RS. Nadir values were significantly different from recovery, siblings 1001±43, and ICU patients 740±98. Conclusion: The observed decrease in RBC-MDA in RS could be explained by decreased substrate (if RBC polyunsaturated fatty acids had undergone peroxidative degeneration) or, less likely, given the low plasma vitamin E, increased antioxidant activity.

Excerpt Elevated erythrocyte ATP is a recently described inherited abnormality in which erythrocytes of some affected individuals contain levels of ATP (6.0 µm/g hemoglobin) twice the normal mean (...