[Arrangement of outer fibrils in Treponema pallidum (Nichols' strain)].
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Microscopy, Electron↗
Biomedical subjects
G Schenk
Publications and source records attributed to G Schenk.
Mechanisms of biopolymer growth: the formation of dextran and levan.
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Bacteria↗
[Enzyme polymerization IX. Kinetics and mechanism of enzymatic synthesis of dextran and effect of acceptors on this reaction].
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Carbon Isotopes↗
[Studies on the fate of injected dextran in the guinea pig].
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Adipose Tissue↗
[On polysaccharide-splitting enzymes in the brush border region of the rat mucosa with special reference to gamma-amylase].
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Amylases↗
[Simple methods for the pharmacologic differentiation of central muscle relaxants].
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Animals↗
Proteolytic and peptidase activities of the jejunum and ileum of the rat during postnatal development.
1. Proteolytic (substrate nitrocasein), tripeptidase (substrate glycylglycylgly-cine) and aminopeptidase (substrate leucyl-beta-naphthylamide) activities were studied in homogenates of jejunal and ileal mucosa of 7-, 10-, 14-, 21-, 35- and 60-day-old rats. 2. Proteolytic activity was practically the same in jejunum of 7-, 10-, 14- and 21-day-old rats, but after day 21 a significant increase was observed. The activity of the ileum changed very little during postnatal development and was always higher than that of the jejunum. 3. Tripeptidase activity was low in the jejunum of 7- and 14-day-old rats, an increase was observed between day 14 and 21, but later no substantial changes were found. There were no changes in the ileum. The activity in the jejunum of 7- and 14-day-old rats was lower than in the ileum, but later the jejunum was more active than the ileum. 4. Aminopeptidase activity had a similar developmental pattern to tripeptidase activity. A low activity was found in the jejunum of 7- and 14-day-old rats, the maximum was in 21-day-old rats and then a decrease was observed, though values for 60-day-old rats were still higher than for 7- and 10-day-old rats. The activity in the ileum was practically the same in all age groups studied except in 14- and 21-day-old rats, where a transient peak was observed.
Aminopeptidases↗
Proteolytic and peptidase activities of the small intestine of human fetuses.
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Aminopeptidases↗
[On localization of peptidase and proteolytic enzyme activities in isolated brush borders of the small intestinal mucosa of rat].
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Aminopeptidases↗
[On localization of alkaline phosphatase in brush borders from the proximal and distal thirds of the small intestine of adult rats and of rat sucklings].
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Albumins↗
[On localization of alkaline phosphatase in brush borders from small intestine of rat].
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Alkaline Phosphatase↗
Activity of beta-galactosidase in homogenates and isolated microvilli fraction of jejunal mucosa from suckling rats.
1. beta-Galactosidase activity was studied in homogenates and isolated microvilli fraction of jejunal mucosa from 14-day-old suckling rats. o-Nitrophenyl beta-d-galactoside served as the substrate. 2. The microvilli fraction contains about one-third of the total activity of the original homogenate. 3. The pH optimum of the beta-galactosidase was 3.5 in the total homogenate and supernatant fraction, whereas in the microvilli fraction the maximum activity was at pH5.5. 4. This work gives further support to the view that two beta-galactosidases exist in the jejunal mucosa.
Animals↗