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- W1982662229 abstract "Two forms of alkaline phosphatase, extracted from human liver and named API1 and API3, are of high molecular mass, but API3 is the larger molecule and is membrane-bound while API1 is smaller and soluble. Enzyme kinetics are identical. It is suggested that API1 is produced from API3 by an endoprotease. We demonstrated the action of an endoprotease in human liver homogenate converting API3 into API1. In the absence of this enzyme no conversion occured. This enzyme is active at an acidic pH (<6.5) in the presence of Ca++ or Mg++ — ions. It is inhibited by traces of EDTA. It is insensitive to diisopropyl fluoro-phosphate, to leupeptin and to reducing or oxidizing chemicals. At alkaline pH (8.6) its activity is rapidly destroyed. The enzyme is stable in acidic buffer. We conclude that API1 is indeed formed from API3 in the living cell by enzymatic conversion." @default.
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- W1982662229 date "1989-04-01" @default.
- W1982662229 modified "2023-09-27" @default.
- W1982662229 title "Endoprotease in human liver transforming multiple forms of alkaline phosphatase" @default.
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- W1982662229 doi "https://doi.org/10.1016/s0009-9120(89)80006-2" @default.
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