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pubmed-article:12883pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:12883pubmed:authorpubmed-author:LamK WKWlld:pubmed
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pubmed-article:12883pubmed:articleTitleBiochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase.lld:pubmed
pubmed-article:12883pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12883pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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