Human placental carboxypeptidase M is anchored by a glycosyl-phosphatidylinositol moiety.
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).
Shimamori
Y
Y
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
Kumagai
Y
Y
Watanabe
Y
Y
Fujimoto
Y
Y
D005260:Female; D058851:GPI-Linked Proteins; D006017:Glycolipids / Q000302:isolation & purification*; D017261:Glycosylphosphatidylinositols; D006801:Humans; D008565:Membrane Proteins / Q000302:isolation & purification; D008666:Metalloendopeptidases / Q000302:isolation & purification; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000302:isolation & purification*; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D012995:Solubility
D058851:GPI-Linked Proteins; D006017:Glycolipids; D017261:Glycosylphosphatidylinositols; D008565:Membrane Proteins; D010716:Phosphatidylinositols; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; C058479:carboxypeptidase M; D008666:Metalloendopeptidases; D043265:Phosphatidylinositol Diacylglycerol-Lyase