|
pubmed:abstractText |
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.
|
