title: Purification and characterization of purple acid phosphatase from rat bone.
abstract: An acid phosphatase, which was immunochemically identical to splenic purple acid phosphatase, was purified to homogeneity from rat bone. The enzyme was a two iron-containing monomeric glycoprotein with a mol. wt of 36,000. The enzyme hydrolyzed aryl phosphates, nucleoside di- and triphosphates, thiamine pyrophosphate, phosphoenolpyruvic acid and acidic phosphoproteins. The enzyme was inhibited by ammonium molybdate, NaF and CuSO4 but not by tartrate and SH-reagents.
mesh_terms: D000135:Acid Phosphatase / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D001842:Bone and Bones / Q000201:enzymology*; D005269:Femur; D005779:Immunodiffusion; D007700:Kinetics; D009928:Organ Specificity; D051381:Rats; D011919:Rats, Inbred Strains; D013053:Spectrophotometry; D013154:Spleen / Q000201:enzymology; D013379:Substrate Specificity; D013977:Tibia
chemical_list: D000135:Acid Phosphatase