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

TitleBiochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase.
Publication TypeJournal Article
Year of Publication1977
AuthorsLam KW, Yam LT
JournalClin Chem
Volume23
Issue1
Pagination89-94
Date Published1977 Jan
ISSN0009-9147
KeywordsAcid Phosphatase, Binding, Competitive, Humans, Hydrogen-Ion Concentration, Kinetics, Lymphatic Diseases, Molecular Weight, Pyrophosphatases, Spleen, Splenic Neoplasms, Tartrates
Abstract

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.

Alternate JournalClin Chem
PubMed ID12883

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