Nov 1, 1975

Human liver acid phosphatases

Hoppe-Seyler's Zeitschrift für physiologische Chemie
D M Rehkop, R L Etten

Abstract

Human liver contains three chromatographically distinct forms of non-specific acid phosphatase (EC 3.1.3.2). Acid phosphatases I, II and III have molecular weights of greater than 200 000, of 107 000, and of 13 400, respectively. Following partial purification, isoenzyme II was obtained as a single activity band, as assessed by activity staining with p-nitrophenyl phosphate and alpha-naphthyl phosphate on polyacrylamide gels run at several pH values. With 50mM p-nitrophenyl phosphate as a substrate, enzymes II and III exhibit plateaus of activity over the pH range 3 - 5 and 3.5 - 6, respectively. Acid phosphatase II is not significantly inhibited by 0.5% formaldehyde. The activity of human liver acid phosphatase II and of human prostatic acid phosphatase towards several substrates is compared. The liver enzyme, is marked contrast to the prostatic enzyme, does not hydrolyze O-phosphoryl choline.

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Mentioned in this Paper

Acid Phosphatase
Choline
Phosphoric Monoester Hydrolases
Polyacrylamide Gels
Enzymes, antithrombotic
Tissue Specificity
Formol
ACPP gene
Prostate
4-nitrophenylphosphate

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