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- W2074611107 abstract "Carboxypeptidase A has been isolated and purified from human pancreas. The procedure involves ammonium sulfate precipitation, O-(diethylaminoethyl) (DEAE)-cellulose, O-(carboxymethyl) (CM)-cellulose column chromatographies and the final purification was 243-fold. Purity was confirmed by disc gel electrophoresis at pH 8.5 and 4.5. The molecular weight of the enzyme was about 35,000 as determined by gel filtration and by disc gel electrophoresis in the presence of sodium dodecyl sulfate. Amino acid analysis of the carboxypeptidase A showed a small number of half-cysteine and methionine residues. The enzyme hydrolyzed substrate hyppuryl-phenyl-lactic acid with a Km of 0.588 mm and a Vmax of 16,665 μmole per minute per milligram. It was inhibited by various metal ions and by heating at 65°C." @default.
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- W2074611107 date "1975-09-01" @default.
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- W2074611107 title "Studies of human carboxypeptidase A purification and properties from human pancreas" @default.
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- W2074611107 doi "https://doi.org/10.1016/0006-2944(75)90027-7" @default.
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