Biochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase.
A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.
D000135:Acid Phosphatase / Q000302:isolation & purification / Q000494:pharmacology*; D001667:Binding, Competitive; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008206:Lymphatic Diseases / Q000201:enzymology*; D008970:Molecular Weight; D011755:Pyrophosphatases / Q000302:isolation & purification / Q000378:metabolism*; D013154:Spleen / Q000201:enzymology*; D013160:Splenic Neoplasms / Q000201:enzymology*; D013644:Tartrates / Q000494:pharmacology*
D013644:Tartrates; D000135:Acid Phosphatase; D011755:Pyrophosphatases