Results 161 to 170 of about 32,792 (197)

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.
Ronald J. T. Pennington, Timothy Edmunds
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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.
Kurt J. Isselbacher, Kurt J. Isselbacher, William D. Heizer, William D. Heizer, Chon R. Shoaf, Chon R. Shoaf   +5 more
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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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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.
Viggo Mohr, Knut Kr. Osnes
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Enzyme‐mediated peptide synthesis using acylpeptide hydrolase

European Journal of Biochemistry, 1991
Acylpeptide hydrolase is shown to catalyse the specific addition of a single amino acid to the N‐terminus of a peptide. The stabilised Sepharose‐coupled form of the enzyme is used to couple a carboxy‐methylated N‐formyl (or N‐acetyl) amino acid to a short pre‐existing peptide.
Alastair Aitken, Anthony D. Auffret, Timothy C. Farries   +2 more
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Purification of a barley peptide hydrolase by disc electrophoresis

Phytochemistry, 1969
Abstract Analytical and preparative disc electrophoresis have been used for further purification of peptide hydrolase A from germinated barley. Its substrate specificity has been reexamined. Peptide bonds with an aromatic amino acid on the carboxyl side of the bond or lysine on the amino side were readily hydrolyzed.
W.C. Burger, Neville Prentice, Mary Moeller   +2 more
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Artificial hydrolase based on carbon nanotubes conjugated with peptides

Nanoscale, 2016
An artificial enzyme was constructed by attaching short peptides with active sites (SHELKLKLKL, WLKLKLKL) onto carbon nanotubes (CNT). It was found that the combination of SHE amino acids was essential to form a catalytic triad. W was also incorporated into this artificial enzyme and acted as a substrate binding site, thus producing an enzyme model ...
Jifeng Liu, Haibo Li, Shuo Wang, Ailing Han, Qingxia Tu, Qiang Zhang, Guozhen Fang, Xingxing He   +7 more
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Peptide‐Based Catalyst Mimicking Hydrolase Enzyme

Journal of Peptide Science
ABSTRACTPeptide‐based nanomolecular constructs offer great possibilities for designing catalytic molecular systems mimicking enzymes. In this study, we designed three tripeptide catalysts that can possibly mimic hydrolase enzymes, with the objective of systematically verifying the scope of modulating enzymatic activity.
Kalpana Kumari, Vivek Prakash, Naveen Kumar, Vibin Ramakrishnan   +3 more
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Partial purification and characterization of barley peptide hydrolases

Phytochemistry, 1968
Abstract Two peptidases from germinated barley were partially purified and characterized. Recycling filtration on dextran gel was used in an improved preparative procedure. BAPA-ase (barley peptide hydrolase A) was found to be inactivated by low pH, mildly resistant to heat treatments and activated by relatively high concentrations (10 −2 -10 −1.3 M)
Neville Prentice, W.C. Burger, Mary Moeller, Jeannine Kastenschmidt   +3 more
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Intestinal Peptide Hydrolases: Peptide and Amino Acid Absorption

Medical Clinics of North America, 1974
Young S. Kim, Kimberly J. Curtis, J. Alex Nicholson   +2 more
openaire   +3 more sources