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In an attempt to identify the secretory mechanism of pancreatic γ-glutamyl transpeptidase (γ-GTP), constant intravenous infusions of secretin alone and in combination with caerulein were performed in anesthetized dogs prepared with a pancreatic fistula. Caerulein produced a marked increase in amylase concentration and only a slight increase in γ-GTP. γ-GTP concentration of the pancreatic juice varied from 12 to 490 mU per ml which ranged up to 188-fold higher than that of the serum. The enzyme concentration depended largely on the flow rate, revealing 3 characteristic curvlinear relationship, regardless of whether caerulein was added to the secretin infusion. No significant relation was demonstrated between amylase concentration and flow rate, amylase and γ-GTP concentrations, and γ-GTP and protein concentration. An inverse linear correlation between γ-GTP and chloride concentrations was obtained when flow rate was below 2.5 ml per 15 min. A significant linear relationship was demonstrated between γ-GTP and leucine aminopeptidase concentrations, and amylase and protein concentrations. The results presented clearly demonstrate that the mechanism of pancreatic secretion of γ-GTP is quite distinct from that of amylase. [ABSTRACT FROM AUTHOR]

A continuous culture apparatus is described, which allows cultivation of photosynthetic bacteria anaerobically in the light and semiaerobically in the dark at constant oxygen tensions. The growth-parameters 1. substrate concentration at half maximum growth rate ( K) and 2. yield ( Y) for Rhodopseudomonas capsulata are calculated. An automatic control system of the oxygen partial pressure in the culture medium is elaborated. It is shown, that the discontinuous regulation with a control unit in connection with two magnetic valves, which give short pulses of either oxygen-free gas or gas mixed with oxygen, is an economic, practicable and reliable method. The yield coefficient Y during growth limited by ammonium sulfate is variable due to the synthesis of nitrogen independent metabolites, such as poly-β-hydroxybutyrate. The storage of poly-β-hydroxybutyrate in continuous culture is a function of both the actual concentration of ammonia and of the C/N ratio. At very low growth rates (1/6 µ) the poly-β-hydroxybutyrate content increases amounting to 33% of the dry weight. In semiaerobically dark grown cells ( pO: 5 mm Hg) the protein and bacteriochlorophyll content increased definitely on dry weight basis with increasing growth rates. In contrast, in anaerobic light cultures only a small increase of the bacteriochlorophyll level but no change of the protein content per dry weight of cells was observed at increasing growth rates. [ABSTRACT FROM AUTHOR]

Quantitative analyses of some organic components of dental calculus, a salivary duct stone, a subgingival calculus and a rhinolith are reported. The protein component of all four calcifications is remarkably similar. It is characterized by high contents of glycine, alanine, glutamic and aspartic acids, and low contents of the sulphur-containing amino acids methionine and cystene. Neither cystine nor hydroxyproline were found, indicating absence of keratin or collagen. The carbohydrate components of dental calculus included rhamnose as major neutral sugar, glucose, galactose, arabinose, mannose, glucosamine, galactosamine and glucuronic acid. The presence of rhamnose suggests bacterial origin for part of the sugar but ribose and deoxyribose were not detected. The salivary duct stone contained less carbohydrate than the other calculi. It contained mainly hexosamine, hexuronic acid and galactose with little glucose and no rhamnose. The rhinolith also contained no rhamnose and the principal sugars were glucose and mannose, with smaller amounts of galactose, arabinose, hexosamine and hexuronic acid. The lipid fraction of dental calculus comprised phospholipids, triglycerides, cholesterol esters and free fatty acid. Of the latter which formed the largest lipid component palmitic, stearic and oleic acids predominated. [ABSTRACT FROM AUTHOR]

Copyright of Pflügers Archiv: European Journal of Physiology is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Calcified Tissue Research is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Calcified Tissue Research is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Calcified Tissue Research is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Calcified Tissue Research is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Calcified Tissue Research is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Calcified Tissue Research is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Calcified Tissue Research is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

An examination of the Cu (II)/wool esr signal intensity variations, together with other relevant copper (II) uptake data, have shown that two types of products are formed during the Cu (II)/wool interaction. One of these gives rise to the observed esr signal, while the other is a diamagnetic sulfide of copper. The latter product arises as a result of a reaction of the metal ion and the products of a water/wool interaction. A reaction scheme consistent with the experi mental observations is suggested. [ABSTRACT FROM PUBLISHER]

The esr spectrum observed from a wool sample treated in a copper (II) solution in the pH range of 1.5 to 5.0 was inter preted by assuming two paramagnetic species each with an effective spin S=1/2. The interaction giving rise to this esr spectrum was ascribed to the complex formation between Cu(II) and the free carboxyl groups in the wool. [ABSTRACT FROM PUBLISHER]

A radiochemical method has been used to follow the course of reaction of formaldehyde with wool. The amount of formaldehyde absorbed from aqueous solutions was dependent on the conditions of treatment. It was found that the pH of the solution, the concentration of formaldehyde in the solution, and the treatment time and temperature markedly affect the extent of the wool-formaldehyde reaction. The presence of salt in the solution has some modifying effect on the uptake of formaldehyde by wool, and there are some apparent differences in the effects of different salts.The amount of formaldehyde bound by the wool was affected by the rinsing conditi ons to which the formalized material was subjected, indicating that not all of the absorbed formaldehyde was present in the form of stable products; this was confirmed by the gradual loss of formaldehyde from formalized wool on exposure to the atmosphere. [ABSTRACT FROM PUBLISHER]

In rabbits fed a diet of pellets containing approximately 12% protein, 4% fat, 44% nitrogen-free extracts and 1% calcium carbonate, serum immunoreactive insulin (IRI) was found to increase to values as high as 1134 μU/ml three hours after the intake of food. After oral glucose (1.75 g/kg), glucose increased by an average of 105 mg% and IRI by 57 μU/ml, whereas after 100 g of pellets these levels increased on the average by 45 mg% and 210 μU/ml, respectively. There was a significant correlation between the IRI levels and the amount of food consumed, and a significant correlation ( P<0.001) between the glucose and IRI levels after intake of food. In rabbits that were fed natural diet such as sugar beet and oats, the increases in glucose and IRI were small. Addition of meat and bone meal as well as the mineral-vitamin supplement containing up to 2 g calcium carbonate caused a considerable increase in glucose and IRI. It is suggested that the high amount of calcium in the feed stimulated the glucose-induced insulin release. [ABSTRACT FROM AUTHOR]

The influence of chlorpromazine (CP) on the incorporation of 3H-uridine into RNA and 3H-histidine into proteins of the optic tectum was investigated in Brachydanio rerio (Teleosts) by means of autoradiography. In addition, the effect of different concentrations of the drug (1-128 mg CP/l bathing medium) on the behaviour of the fish was examined. The LD was 2 mg CP/l. 1.5 mg CP/l, a sublethal dose which induces behaviour changes, slightly inhibited RNA synthesis. On the other hand, the same dose has a marked effect on protein metabolism; both total incorporation of 3H-histidine into the cell bodies as well as protein breakdown in the nerve fibres appeared to be inhibited as indicated by a decreased labelling of the pericarya after short periods and an increased accumulation of label in the nerve fibres after long periods of incorporation. Moreover the 3H-histidine labelling in the optic tectum was less affected by exogenous protease in CP-treated animals than in controls. The possible sites of action of the drug are discussed. [ABSTRACT FROM AUTHOR]

Copyright of Ricerca in Clinica E in Laboratorio is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Klinische Wochenschrift is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The distribution of labeled protein along the pigeon retino-tectal pathway was studied with light microscopic autoradiography after intraocular injection of H-l-leucine. Evidence was found that proteins synthesized in the ganglion cell perikarya migrate in the axoplasm. Some data suggested that two separate molecular waves reached regions rich in synaptic endings in the early phase after injection. Their respective speed of migration would be 100-500 mm/day and 20-60 mm/day. The most heavily labeled wave, advancing at a speed of 1-2 mm/day, was detected during the late phase after injection. [ABSTRACT FROM AUTHOR]

Axoplasmic transport of labelled proteins was studied in the vagus and hypoglossal nerves of the adolescent rabbit after an intramedullary injection of H-leucine. As demonstrated by radioautography, the incorporated activity found in the intramedullary axons had a perikaryal origin and was transported distally at a rate of several mm per hour. The migration of labelled proteins along the axons outside the medulla was followed by measuring the specific radioactivity of the proteins in the hypoglossal and vagus nerves. A rapid transport of labelled proteins in proximo-distal direction was demonstrated at rates of 16-17 mm/h in the vagus nerve and 10-15 mm/h in the hypoglossal nerve. The effect of puromycin and nerve ligature on the rapidly moving component is described. [ABSTRACT FROM AUTHOR]

After H-lysine was applied to the X and XII cranial nuclei, radioactive protein synthesized in the nerve cell bodies of the hypoglossal and vagus nerves moved down the axons of these fibers at maximal rates of 6.3±1.2 and 16±3 mm per day, respectively. The distribution of radiolabeled protein at various periods indicated that other proteinaceous components moved at slower velocities. [ABSTRACT FROM AUTHOR]

Two experiments have been performed to gain insight into the mechanisms of axoplasmic protein migration. In the first the concentration of protein along cat optic nerves was measured to determine if a concentration gradient was present which might drive protein in a proximo-distal direction. None was found. In the second experiment we endeavored to determine if axonal protein migration would continue despite cycloheximide-induced inhibition of protein synthesis in the cell body. It did continue to migrate and with no significant change in rate (0.8-1.0 mm/day). It is concluded that these experiments rule out diffusion down a proximo-distal concentration gradient as a mechanism for axonal protein migration. [ABSTRACT FROM AUTHOR]

Copyright of Zeitschrift Für Die Gesamte Experimentelle Medizin Einschließlich Experimentelle Chirurgie is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Comparison of the skeletal muscles from vitamin E-deficient and control rabbits showed that the muscles from the deficient animals had lower contents of protein and glycogen but more water and lipid. Increases of individual lipids per unit weight of muscle from deficient animals compared with those from control animals were 2.2-fold for gangliosides, 2.18-fold for cholesterol, 1.74-fold for sulfatides, and 1.45-fold for neutral glycosylceramides. Total phospholipids did not change; this was the result of an increase in sphingomyelin (1.47-fold) and a decrease of phosphatidylcholine to 83% of the control, while the other fractions remained unchanged. When the measurements were referred to total muscle, the contents of cholesterol, gangliosides, sulfatides, neutral glycosylceramides, and sphingomyelin in muscle from vitamin E-deficient rabbits were also above those of the control rabbits, and only the phoshatidylcholine content was decreased. It was not possible to determine whether the alteration of lipid content preceded or followed the onset of signs of muscular dystrophy.

A fim de determinar os valores normais de concentração proteica na urina, em amostra de população sadia, foi usada uma reação de biureto, em 62 amostras de urina coletadas ao acaso. A concentração proteica média em todo o grupo foi de 6,0mg% (± 3,2) com a amplitude de 2,0 - 14,5mg%. Tais resultados concordam com aqueles previamente relatados na literatura.In order to determinate the normal values for urine protein concentration in one sample of healthy population it was used a biuret reaction in 62 urine samples collected at random. The mean protein concentration in the whole group was 6.0mg% (SD ±3.2) with a range of 2.0 - 14.5mg%. Those results agreed with the previously reported, in the literature.

Myelin was isolated from the brains of “quaking” and littermate control animals and its composition was determined. The brains of quaking animals contained approximately one-fourth as much myelin as the control animals. There were qualitative as well as quantitative differences between the myelin from the two groups. By continuous cesium chloride gradient flotation it was shown that the myelin from the quaking animals consisted solely of a band corresponding to the heavier and smaller of the two bands found in normal controls. Cholesterol and glycolipids were lower and phospholipids (mainly phosphatidylcholine) and protein were higher in quaking animals than in controls. Also, phosphatidalethanolamine was decreased, and several consistent differences in the fatty acids (both unsubstituted and hydroxy) and aldehydes of the component lipids were found. In general there were smaller amounts of monounsaturated fatty acids in quaking animals. We suggest from these findings that myelin in the quaking mouse has certain compositional similarities with juvenile myelin, but it may be an abnormal type of myelin.

A razão nitrogênio ureico/creatinina (N u/c) foi medida em indivíduos de ambos os sexos nos grupos de 3 a 10 anos, 11 a 15 anos e acima de 15 anos de idade, em uma amostra das populações das comunidades de Vila de Icapara, Pontal do Ribeira e diaristas de Iguape, localizadas no litoral sul de São Paulo, no Vale do Ribeira. Foi calculada a adequação do consumo de proteínas entre as famílias, através dos resultados de um inquérito alimentar feito pelo método das pesagens. Partiu-se da hipótese de que haveria maior proporção de indivíduos com a razão N u/c maior ou igual a 5 nas famílias que apresentaram consumo proteico maior ou igual a 80,0% de adequação; através do teste chi2; 0,05, obteve-se uma associação entre a adequação do consumo de proteínas nas famílias e a razão N u/c nos indivíduos das respectivas famílias.A study of ureic nitrogen/creatinine ratio in individuals of both sexes from 3 to 10 years, 11 to 15 years and over 15 years age groups, was carried out on a sample of coastal populations from Vila de Icapara, Pontal do Ribeira and the city of Iguape, all of them located in the south of the State of S. Paulo, Brazil. Adequate protein consumption of each family was calculated from the results of a nutrition survey using weighing procedure. Applying the chi2 test chi2; 0,05 a correlation of adequate family consumption and ureic nitrogen/creatinine ratio was encountered.