Search results for "Phosphoglycolate phosphatase"
showing 2 items of 2 documents
Phosphotransferase properties of human erythrocyte phosphoglycolate phosphatase.
1982
Abstract 1. 1. Human erythrocyte phosphoglycolate phosphatase (PGP) (EC 3.1.3.18) shows transferase properties. Using p -nitrophenylphosphate ( p -NPP) as substrate, methanol, at a concentration of 4.9 M. was the most efficient phosphate acceptor tested (60% phosphate transfer). 2. 2. The branched alcohols i -propanol and i -butanol accept the phosphate better than the unbranched compounds. The acceptor potency is methanol > ethanol > i -propanol > n -propanol > i -butanol > n -butanol. 3. 3. The relative transferase activity could be demonstrated to be independent of substrate concentration, pH. and the inhibitory effect of NaF at 2 and 4 mM. 4. 4. POP shows no transferase activity towards…
Purification, isolation and characterization of a phosphoglycolate phosphatase isoenzyme from human erythrocytes.
1982
1. Preparation, purification and characterization of a phosphoglycolate phosphatase (PGP) isoenzyme from human erythrocytes was achieved by DEAE-Sepharose CL-6B chromatography and isoelectric focusing using carrier ampholytes, pH 4-6. 2. The isoenzyme has an isoelectric point of 5.00 +/- 0.05 and could be purified 33,000 fold to a specific activity of 32.7 U/mg of protein. It represents the PGP phenotype 1 consisting of a single isoenzyme. 3. The enzyme is composed of two subunits (mol. wt 35,000) which are identical and not connected by SS-bridges. 4. At 4 degrees C the isoenzyme is more stable in the pH range of 7-9 than at acid pH values. 5. Incubation at 30 and 40 degrees C for 4 hr doe…