Immunological and biochemical evidence for identity of tartrate-resistant isoenzymes of acid phosphatases from human serum and tissues.
We purified acid phosphatase isoenzyme 5b from a human spleen affected by leukemic reticuloendotheliosis and used it to produce a specific antiserum. The antiserum was used to show complete immunological identity among isoenzymes 5a and 5b in human serum, and 5b isolated from a giant-cell bone tumor and from the spleen of a case of Hodgkin's disease. Acid phosphatase 5b in a giant-cell bone tumor was isolated for biochemical characterization. Its pH optimum and substrate specificity were very similar to those of isoenzyme 5b from human spleen.
D000135:Acid Phosphatase / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D001842:Bone and Bones / Q000201:enzymology; D006689:Hodgkin Disease / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007527:Isoenzymes / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D007943:Leukemia, Hairy Cell / Q000201:enzymology*; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity; D013644:Tartrates / Q000494:pharmacology
D007527:Isoenzymes; D013644:Tartrates; D000135:Acid Phosphatase