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      Human placental carboxypeptidase M is anchored by a glycosyl-phosphatidylinositol moiety.

      1 , , ,
      Biochemistry international

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          Abstract

          Basic carboxypeptidase activity was released from human placental membranes on treatment with phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis. The enzyme was successively purified to homogeneity by SDS-polyacrylamide gel electrophoresis. The molecular nature and some catalytic properties of the purified enzyme revealed that it is identical with recently described basic carboxypeptidase M (R.A. Skidgel et al. J. Biol. Chem. 264 (4) 1989 2236-2241).

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          Author and article information

          Journal
          Biochem. Int.
          Biochemistry international
          0158-5231
          0158-5231
          1990
          : 20
          : 3
          Affiliations
          [1 ] Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
          Article
          2161229
          c3075315-dffb-4908-876d-6b1ec10b845d
          History

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