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Sesquiterpenoid Hormones Farnesoic Acid and Methyl Farnesoate Regulate Different Gene Sets in Shrimp <i>Neocaridina davidi</i> Hepatopancreas. [PDF]
BiomoleculesLuan Y, Nong W, So WL, Hui JHL.
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Metal ion requirement of goat carboxypeptidase B.
Indian journal of biochemistry & biophysics, 1977 M P, Rao, R D, Dua
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By-product analogs for bovine carboxypeptidase B
Biochemistry, 1978A series of monocarboxylic and dicarboxylic acid sulfur-containing by-product analogues of lysine and arginine has been synthesized and tested as competitive inhibitors of bovine carboxypeptidase B. The most effective derivatives were guanidinoethylmercaptosuccinic acid and aminopropylmer-captosuccinic acid with Kis of 4 and 8 X 10(-6) M, respectively.
T J, McKay, T H, Plummer
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Determination of carboxypeptidase B in duodenal contents
Clinica Chimica Acta, 1972Abstract A rapid and simple method for the estimation of carboxypeptidase B activity in 10 μl of duodenal contents is described. The arginine liberated from hippuryl-arginine is determined at 546 nm by reaction with benzoquinone within 20 min. Bile pigments and proteins are removed by trichloroacetic acid precipitation.
K, Lorentz, B, Flatter
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Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substrates
Bioorganic & Medicinal Chemistry Letters, 1999Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B. The catalytic reaction is readily monitored spectrophotometrically by disappearance of the intense absorption (348.5 nm, epsilon 18400) of the azo chromophore, which chemically fragments after substrate ...
W L, Mock, D, Xu
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Radiometric assay for carboxypeptidase H (EC 3.4.17.10) and other carboxypeptidase B-like enzymes
Analytical Biochemistry, 1989Carboxypeptidase H, EC 3.4.17.10, also known as enkephalin convertase, carboxypeptidase E, and crino carboxypeptidase B, is an important enzyme involved in the biosynthesis of bioactive peptides. To assay the enzyme, tissues are homogenized in at least 20 vol (ml/g) of 0.025 M Tris-HCl buffer, pH 8, with 5 mg/ml of bovine serum albumin.
J, Rossier +3 more
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[21] Carboxypeptidases A and B
1972Publisher Summary The carboxypeptidases that have been used extensively for structural studies are the pancreatic carboxypeptidases A and B. The A enzyme (CPA) removes C-terminal aromatic and long side-chain aliphatic residues most rapidly, and removes glycine and acidic amino acids only slowly.
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