Purification and characterization of purple acid phosphatase from rat bone.
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.
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
D000135:Acid Phosphatase