Abstract
The carboxypeptidase B of human small intestine has been purified and partially characterized. The enzyme was purified by ammonium sulfate precipitation, DEAE-cellulose, CM-cellulose, and Sepharose 6B column chromatography. Purity was confirmed by disc gel electrophoresis at pH 8.5. The enzyme was purified 412-fold over the crude extract. Molecular weight of the enzyme was about 24000, as determined by Sephadex column chromatography and disc gel electrophoresis with sodium dodecyl sulfate. The enzyme was immunologically different from human pancreatic carboxypeptidase B 1 and B 2b since it does not cross-react with antiserum elicited against pure human pancreatic carboxypeptidase B 1. Extraction of the insoluble precipitate of intestinal wall yielded a carboxypeptidase which is possibly the dimer of carboxypeptidase B. The carboxypeptidase hydrolyzed HLA, HLL, and HLAa substrates. The enzyme was activated by Cd 2+ and Hg 2+. It was inhibited by heated SDS and urea. The enzymes were not inhibited or activated by Zn 2+, EDTA, and 2-mercaptoethanol.
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