The membrane-bound basic carboxypeptidase from hog intestinal mucosa1Enzymes: carboxypeptidase B (EC 3.4.17.2); carboxypeptidase D (EC 3.4.17.-); carboxypeptidase H (EC 3.4.17.10); carboxypeptidase M (EC 3.4.17.12); carboxypeptidase N (EC 3.4.17.3).1
نویسندگان
چکیده
منابع مشابه
Carboxypeptidase
is attacked, it is clear that the substrate of carboxypeptidase need not have a free amino group nor need it, ~ despite the name of the enzyme, be a pepfide. I t has been assumed, but not proven experimentally, that chloracetyl-tyrosine is attacked by only a single enzyme and that the same enzyme which attacks chloracety!-tyrosine also attacks the other supposed substrates of carboxypepfidase. ...
متن کاملHuman carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones.
A membrane-bound neutral carboxypeptidase B-like enzyme was solubilized from human placental microvilli with 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) and purified to homogeneity by ion-exchange chromatography and affinity chromatography on arginine-Sepharose. It gave a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent Mr of 62,00...
متن کاملKinetic and Mechanistic Studies on Carboxypeptidase a (ec 3.4.1 2.2) from Goat Pancreas
The molecular weight of goat carboxypeptidase A was found to be approximately 34,600 by Gel-filtration and SDSmethod. It was found to be a zinc-metalloprotein both by chemical and emission spectroscopy methods, having one atom of zinc per protein molecule. Removal of zinc either by cJis...1.ysis at pH 6.0 or below and by the use of thelating agents at neutral pH, yislded an inactive apocarlooxy...
متن کاملCarboxypeptidase A
Scientific and technological advances brought about in the recent part of this decade have provided great insight regarding the catalytic mechanism of the prototypical zinc-requiring protease carboxypeptidase A (CPA). Importantly, some of our ideas regarding the general theory of enzyme catalysis have been inspired and developed through studies of this enzyme. Just as importantly, CPA serves as...
متن کاملCarboxypeptidase from Yeast
In order to render the carboxypeptidase from yeast more readily available for use in sequence studies in protein chemistry, the procedure of Hata, Hayashi, and associates for the preparation of the enzyme has been adapted to a larger scale through cooperation with the New England Enzyme Center. From 100 pounds of bakers’ yeast, the yield was about 1.4 g of the chromatographically purified, elec...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 1999
ISSN: 0005-2736
DOI: 10.1016/s0005-2736(99)00122-4