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- W1750465523 abstract "The activity of carboxypeptidase A [EC 3.4.12.2] was inhibited by 3-phenylpropionate derivatives (p-aminocinnamate, 3-p-aminophenylpropionate and 3-p-acetylaminophenylpropionate), and to investigate its use as a ligand for affinity chromatography 3-p-aminophenylpropionate was directely and indirectly coupled to Sepharose 4B. carboxypeptidase A was adsorbed only on 3-p-aminophenylpropionate bound to the gel through p-phenylenediamine as a spacer. Carboxypeptidase A from pancreas was purified by a combination of this affinity adsorbent and ion exchange chromatography. The purified carboxypeptidase A had a homogeneity similar to that of a commercial product, as judged by disc gel electrophoresis. The carboxypeptidase activity of Pronase was slightly retarded on the gel column, but could not be separated from its caseinolytic activity. Angiotensin I-converting enzyme [peptidyl dipeptidy hydrolase, EC 3.4.15.1] obtained from hog kidney cortex was not bound to the gel." @default.
- W1750465523 created "2016-06-24" @default.
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- W1750465523 date "1977-05-01" @default.
- W1750465523 modified "2023-10-18" @default.
- W1750465523 title "Purification of Carboxypeptidase A Using Sepharose 4B-Bound 3-Phenylpropionate" @default.
- W1750465523 cites W1566830427 @default.
- W1750465523 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a131581" @default.
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- W1750465523 hasPublicationYear "1977" @default.
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