Kinetic properties of tartrate-resistant acid phosphatase isolated from human spleen with leukemic reticuloendotheliosis.
The tartrate-resistant acid phosphatase was isolated from the spleen of a patient with leukemic reticuloendotheliosis. The unique characteristic of the enzyme is its similar reactivity toward p-nitrophenylphosphate, inorganic pyrophosphate ADP, and ATP. When ATP was incubated with the enzyme, the initial products were ADP and inorganic phosphate. The kinetic data confirmed that these substrates were hydrolyzed by the same enzyme. This type of substrate specificity is clearly different from acid phosphatase and pyrophosphatases previously described in the literature.
D000135:Acid Phosphatase / Q000378:metabolism*; D000227:Adenine Nucleotides / Q000378:metabolism; D001665:Binding Sites; D006801:Humans; D007700:Kinetics; D007938:Leukemia / Q000201:enzymology*; D008206:Lymphatic Diseases / Q000201:enzymology*; D009578:Nitrobenzenes / Q000378:metabolism; D013154:Spleen / Q000201:enzymology*; D013644:Tartrates / Q000494:pharmacology
D000227:Adenine Nucleotides; D009578:Nitrobenzenes; D013644:Tartrates; D000135:Acid Phosphatase