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The protective effect of African IgG antibodies against Plasmodium falciparum malaria was investigated by passive transfer in Thai patients. Sera from 333 African adults were collected in the Cote d'Ivoire and subjected to extensive screening. One hundred fifty-three samples were discarded for safety reasons, and IgG was extracted from those remaining under conditions allowing their use by the intravenous (iv) route. Eight Thai patients with P. falciparum parasitemia were treated by iv inoculation of the IgG: six with a 100 mg/kg dose given over three days, one with a single 20 mg/kg dose, and one with a single 200 mg/kg dose. To ensure a safety margin of at least 48 hours, subjects were chosen among patients having a recrudescent parasitemia following quinine treatment failure at the RI level. At that stage, symptoms were mild or absent and parasitemia was low but increasing (range 4, 200-9,000/microliters). The IgG pool exerted a profound, stage-specific, but non-sterilizing effect on each of the strains tested, and proved to be safe. Asexual parasitemia decreased by a mean 728-fold (range 46-1,086), while gametocytes were unaffected. Clearance of parasites and symptoms was as fast or faster than with drugs, and was consistent in the eight patients treated, suggesting that target antigens were equally expressed in geographically remote isolates. In peripheral blood smears, no mature forms were seen at any time during the followup, which does not support the hypothesis that reversal of cytoadherence occurred. After the disappearance of the transferred antibodies, recrudescent parasites from three patients were found to be susceptible to the same extent (mean decrease of 1,310-fold) to the same IgG preparation, indicating that selection of parasites able to escape the effect of antibodies had not occurred. No adverse side-effects were detected during the followup, which lasted one year.

A controlled study concerning the surgical use of a fibrin glue was conducted in 50 patients undergoing partial pulmonary excision. In 25 of these patients, chosen at random, hemostasis and aerostasis of the fissural, and/or intersegmentary dissection planes were achieved by electrocoagulation, in the other 25 by the application of fibrin glue. The statistical study did not show any significant difference between the two groups in terms of the surgical indication, the type of excision and the associated surgical procedures (pleurectomy and parietectomy). No significant statistical difference was observed concerning the quality of aerostasis, the post-operative drainage, the persistance of residual collection or faulty reexpansion after removal of the latter, and the necessity for repeated drainage. The same applied to the length of post-operative hospital stay. This study seems to demonstrate that the surgical application of fibrin glue on the fissural and/or intersegmentary dissection planes is feasible but, as compared to electrocoagulation, does not significantly improve the quality of the surgical results for partial pulmonary excision; however its use could reduce the duration of post-operative drainage.

Glutenin subunits from nullisomic-tetrasomic and ditelocentric lines of the hexaploid wheat variety 'Chinese Spring' (CS) and from substitution lines of the durum wheat variety 'Langdon' were fractionated by reversed-phase high-performance liquid chromatography (RP-HPLC) at 70 °C using a gradient of acetonitrile in the presence of 0.1% trifluoroacetic acid. Nineteen subunits were detected in CS. The presence and amounts of four early-eluted subunits were found, through aneuploid analysis, to be controlled by the long arms of chromosomes 1D (1DL) (peaks 1-2) and 1B (1BL) (peaks 3-4). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that these four subunits are the high molecular weight subunits of glutenin, which elute in the order 1Dy, 1Dx, 1By, and 1Bx. Similar amounts of 1DL subunits were present (6.3 and 8.8% of total glutenin), but 1BL subunits differed more in abundance (5.4 and 9.5%, respectively). Results indicate that most late-eluting CS glutenin subunits were coded by structural genes on the short arms of homoeologous group 1 chromosomes: 6 by 1DS, 5 by 1AS, and 4 by 1BS. Glutenin of tetraploid 'Langdon' durum wheat separated into nine major subunits: 6 were coded by genes on 1B chromosomes, and 3 on 1A chromosomes. Gene locations for glutenin subunits in the tetraploid durum varieties 'Edmore' and 'Kharkovskaya-5' are also given. These results should make RP-HPLC a powerful tool for qualitative and quantitative genetic studies of wheat glutenin.

alpha 1-Antitrypsin (AAT) has been purified from human plasma supernatant A (equivalent to COHN fraction II + III) by a large-scale chromatographic procedure involving anion-exchange adsorption on DEAE Sepharose CL-6B fast flow and size-exclusion chromatography on Sephacryl S-200. Before freeze-drying, the liquid concentrate was heat-treated at 60 degrees C for 10 h to reduce the risk of transmission of blood-born viral diseases. Using this procedure, AAT is recovered with 80-90% purity in 65-75% yield from supernatant A. The heterogeneity of AAT is preserved across the purification steps. In addition, purified AAT exhibits inhibitory activities against trypsin and elastase equivalent to that of the serum protein. The mean association rate constant for elastase was found as high as 2.15 X 10(5) M-1 s-1. Thus, purifying active AAT from supernatant A contributes to improving the availability of this protein which may be potentially useful in the treatment of hereditary emphysema.

We report here a simple procedure for the isolation of human plasma fibronectin by affinity adsorption on a new lyophilized adsorbent which is obtained by mixing and polymerizing agarose with gelatin. This method permits to obtain fibronectin and a fibronectin-depleted plasma without dilution. The yield of fibronectin is about 20 to 25 per cent. Fibronectin was identified by cross-reactions against specific antibodies. Its purity (greater than or equal to 99 per cent) was controlled by immunoelectrophoresis and SDS-PAGE. Furthermore, its biological activity was demonstrated by a spreading test performed on BHK cells. Such a test can be used to determine the specific activity of extracted fibronectin considering that the number of spread cells placed in presence of exogenous fibronectin (5 microgram/ml of culture medium) was 4.5 to 5 fold-superior to the control, after 30 minutes of incubation at 37 degrees C.

Gliadin proteins of the hexaploid wheat variety 'Chinese Spring', and of its nullisomic-tetrasomic and ditelocentric aneuploid lines, were analyzed by reversed-phase high-performance liquid chromatography (RP-HPLC). Reversed-phase separations were carried out at 70°C on C8 and C18 columns using a gradient of increasing acetonitrile concentration in the presence of 0.1% trifluoroacetic acid. Thirty-five components were separated and all were found to be controlled by genes on the short arms of group 1 and group 6 chromosomes (the complex Gli-1 and Gli-2 loci). Results indicated that gluten polypeptides elute as groups in order of increasing hydrophobicity in the following approximate order: (1) albumins plus globulins, (2) ω-gliadins, (3) high molecular weight (MW) glutenin subunits, (4) α-type gliadins, (5) low MW glutenin subunits, and (6) γ-gliadins. The three distinct protein types coded by genes at the complex Gli-I loci (ω-gliadins, γ-gliadins, and low MW glutenin subunits) thus have uniquely different surface hydrophobicities. Similarly, gene locations for hexaploid 'Cheyenne' gliadins and durum gliadin proteins in the varieties 'Langdon', 'Edmore', and 'Kharkovskaya-5' were determined through RP-HPLC analysis of aneuploid lines. All results confirm known locations of genes for gliadin proteins, and demonstrate that RP-HPLC is a powerful new tool for analysis of gliadins in breeding and genetic studies.

The subunit composition of glutenin from 47 European wheat cultivars was studied using SDS-polyacrylamide gel electrophoresis. These cultivars are genetically related since they originate from the same stock. Moreover, the diversity of sample, containing cultivars with very different French bread-making qualities, makes it possible to investigate the relationship between glutenin subunit composition and bread-making quality. 16 electrophoretic types of glutenin subunits could be distinguished: these were grouped into four classes. Depending on the cultivar, six to eight glutenin subunits with MW more than or equal to 62,000 were detected. Subunits 3 and 5, with an approximate MW of 122,000 and 108,000 respectively, seem to play a prominent role on bread-making quality; they were found in cultivars of good quality and were absent in those unsuitable for making French bread. Two other subunits (9 and 10; MW: 71,000 and 66,000, respectively) have a less defined influence but may be needed in some types of glutenin structure. Aneuploid analysis shows that in 'Chinese Spring', subunit 5 is coded by a gene on the long arm of chromosome 1B. The location of genes coding for subunits 3, 9 and 10 could not be determined.

Methods to inactivate (or eliminate) viruses must be developed to ensure the safety of blood plasma fractions. For that purpose, dry or liquid heat treatment, solvent/detergent mixtures, beta-propiolactone/ultraviolet treatment, and chromatographic methods are the main procedures in use to date.

Ten pairs of reciprocal crosses have been made between wheat cultivars which show differences in their glutenin subunit compositions. The F1 seed glutenin subunit composition was studied by means of polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (SDS). The results indicate that all the high molecular weight (HMW) and medium molecular weight (MMW) subunits (from 133,000 to 65,000 daltons) are transmitted to the F1 seed generation from the parental cultivars. In accordance with the triploid nature of the heterozygous endosperm (3n) and with the maternal and paternal gene dosage ratio (2∶1) in the endosperm itself, a significant effect of maternal parent is registered when comparing pairs of reciprocal seeds. Genes coding for the glutenin subunits are expressed whatever their doses are (one, two, or three) in the hybrid endosperm; thus the glutenin subunits inheritance is consistent with the co-dominant type.For one pair of the reciprocal crosses, two MMW parental bands (MW: 71,000 and 66,000) seemed absent in the F1 seed patterns while a new band with an intermediate, apparent MW (68,000) appears. This phenomenon was observed when the glutenins analyzed by electrophoresis were previously separated from other endosperm proteins, and not when they were directly extracted from the ground seed. We assume that the extraction can cause interactions between moieties attached to the subunits and lead to the formation of a complex having an intermediate electrophoretic mobility.

We describe a large-scale chromatographic method to purify alpha 1-antitrypsin (AAT) from human plasma supernatant II + III. Supernatant II + III was injected onto DEAE sepharose CL 6B to get an albumin-rich fraction as well as a fraction that contained about 45% AAT. This intermediate purity AAT fraction was further purified by size-exclusion chromatography on Sephacryl S-200. The product was heated in solution at 60 degrees C for 10 hours in the presence of a stabilizer to lower the risk of transmission of viral diseases. Purity of the AAT concentrate is over 85%; clinical testing of its safety and efficacy in the treatment of PiZ patients is underway.