Studies of the heterogeneity of carp liver acid phosphatases: acid phosphatase--I. Subunit structure and carbohydrate composition.
The three molecular forms of the carp liver acid phosphatase (AcPase) were shown to be dimeric proteins, two of them differing in molecular weights. An activating effect of ConA binding on the AcPases has been observed. AcPase I and AcPase II showed a mol. wt of 122,500 and of 58,884 +/- 3000 for their subunits. It is assumed that AcPase I is a sialylated derivative of AcPase II. AcPase III has a mol. wt of 93,132 and the two subunits of 46,556 +/- 4000. A homogeneous AcPase I was obtained and its carbohydrate composition is presented.
D000135:Acid Phosphatase / Q000302:isolation & purification*; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002347:Carps; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight
D002241:Carbohydrates; D046911:Macromolecular Substances; D000135:Acid Phosphatase