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Clinical Chemistry 23: 89-94, 1977;
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Clinical Chemistry, Vol 23, 89-94, Copyright © 1977 by American Association for Clinical Chemistry

Biochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase

KW Lam and LT Yam

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.


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Home page
 Am. J. Physiol. Cell Physiol.Home page
R. A. Terkeltaub
Inorganic pyrophosphate generation and disposition in pathophysiology
Am J Physiol Cell Physiol, July 1, 2001; 281(1): C1 - C11.
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