Showing papers on "Purple acid phosphatases published in 1986"
TL;DR: Red kidney bean phosphatase shows a marked preference for ATP as substrate over p-nitrophenyl phosphate and ADP, and stable esters such as AMP and β-glycerophosphate are very poor substrates.
130 citations
59 citations
TL;DR: Tartrate-resistant acid phosphatase active on nucleoside di- and triphosphate substrates was isolated from developing rat bone and purified 2500-fold with a purple coloration and activity that was sensitive to reducing agents.
47 citations
TL;DR: An acid phosphatase, which was immunochemically identical to splenic purple acid phosphate, was purified to homogeneity from rat bone and hydrolyzed aryl phosphates, nucleoside di- and triphosphates, thiamine pyrophosphate, phosphoenolpyruvic acid and acidic phosphoproteins.
Abstract: 1. 1. An acid phosphatase, which was immunochemically identical to splenic purple acid phosphatase, was purified to homogeneity from rat bone. 2. 2. The enzyme was a two iron-containing monomeric glycoprotein with a mol. wt of 36,000. 3. 3. The enzyme hydrolyzed aryl phosphates, nucleoside di- and triphosphates, thiamine pyrophosphate, phosphoenolpyruvic acid and acidic phosphoproteins. 4. 4. The enzyme was inhibited by ammonium molybdate, NaF and CuSO4 but not by tartrate and SH-reagents.
21 citations
TL;DR: Colorimetric and radiochemical experiments indicate the presence of one mole of tightly bound phosphate in the oxidized (purple) form of the purple acid phosphatase; this phosphate is released upon reduction.
18 citations