Results 251 to 260 of about 60,986 (298)
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Peptide hydrolase activities in rat muscle cultures

International Journal of Biochemistry, 1978
Abstract 1. 1. The specific activity of acid proteinase, cathepsin B1, arylamidase and cathepsin C was much higher in 2-day cultures of rat muscle than in mature muscle. Alkaline proteinase showed little or no difference. 2. 2. The total and specific activity of the enzymes, except alkaline proteinase, increased when the cultures were grown ...
M E, Parsons   +2 more
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Rapid colorimetric assay for intestinal peptide hydrolases

Analytical Biochemistry, 1974
Abstract A simple two-step method is described for quantitating the release of free l -phenylalanine, l -leucine, l -methionine, or l -isoleucine from di- or polypeptides. The colorimetric assay is based on the ability of l -amino acid oxidase to catalyze the oxidation of free l -amino acid, but not of peptides.
C R, Shoaf   +2 more
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Photothermally switchable peptide nanostructures towards modulating catalytic hydrolase activity

Nanoscale, 2021
The Aβ42 amyloid-inspired peptide fragment renders pathway-driven self-assembled nanostructures mediated by heat, light and chemical cues. They are envisaged as robust biocatalysts with remarkable variation of the hydrolase catalytic efficiency.
Ashmeet Singh   +5 more
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Lysosomal hydrolases of the epidermis.

British Journal of Dermatology, 1975
Four distinct peptide hydrolases (EC 3-4) have been characterized in guinea-pig epidermis; these are cathepsin B1, cathepsin C, cathepsin D and arylamidase. Their properties are consistent with those of lysosomal enzymes. Cathepsin E was not detected.
P D, Mier, J J, van den Hurk
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Characterization of an acid-stable peptide hydrolase and of peptide hydrolase a in germinated wheat

Phytochemistry, 1969
Abstract Peptide hydrolase A from germinated wheat has been separated from an acid-stable peptide hydrolase. The stability of these enzymes to pH and temperature and their K m values are described. Some peptides hydrolyzed by the acid-stable enzyme are reported.
Neville Prentice   +3 more
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Peptide hydrolases in holothurian intestinal mucosa

Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1981
Abstract 1. Peptide hydrolases from intestinal mucosa of H. forskali and N. mixta were studied by starch gel electrophoresis. 2. Dipeptides hydrolyzed were L -Leu- L -Leu and L -Gly- L -Leu. L-Gly- L -Tyr and L -Leu- L -Tyr were not 3. L -Leu- L -Leu- L -Leu-was hydrolyzed by extracts of both species. 4.
S. McGettigan   +3 more
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A high-molecular weight peptide hydrolase in erythrocytes

International Journal of Biochemistry, 1982
1. A peptide hydrolase has been partially purified from the soluble fraction of erythrocyte lysates. 2. The enzyme has a molecular weight of approximately 600,000 and hydrolyses the chymotrypsin substrate glutaryl-Gly-Gly-Phe-7-amido-4-methylcoumarin (pH optimum 7.0) and the trypsin substrate CBZ-Gly-Gly-Arg-2-naphthylamide.
T, Edmunds, R J, Pennington
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Peptide hydrolases in cotyledons of germinating lupin

Phytochemistry, 1993
Abstract Aminopeptidase (AP), carboxypeptidase (CP) and endopeptidase (EP) activities have been analysed in extracts prepared from cotyledons of dry and five and 14 days-germinated lupin seeds ( Lupinus albus ). At these three stages the pattern of the enzymatic activities change in a complex manner.
Isabel C. Duarte   +2 more
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Peptide hydrolases of Antartic krill, Euphausia superba

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1985
Abstract 1. 1. A survey has been made of the peptide hydrolase activities occurring in Antarctic krill, Euphausia superba. 2. 2. A major protein hydrolyzing activity in the pH range of 6–8, and a minor activity at pH 3–4, were detected. 3. 3. Temperature optima of approx.
Knut Kr. Osnes, Viggo Mohr
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Developmental Changes in Peptide-Bond Hydrolases

1970
The rapid growth of brain during ontogeny affords a valuable experimental tool for studying the factors affecting protein breakdown and turnover. Despite the wealth of information documenting the remarkable changes during developmental(1–5) the correlation between chemical events and functional changes is poorly understood.
Neville Marks, Abel Lajtha
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