title: Purification, isolation and characterization of a phosphoglycolate phosphatase isoenzyme from human erythrocytes.
abstract: 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 does not affect the activity of the isoenzyme. 6. It has a Km-value of 0.28 mM for phosphoglycolate (PG) as substrate.
mesh_terms: D004912:Erythrocytes / Q000201:enzymology*; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007527:Isoenzymes / Q000097:blood*; D007700:Kinetics; D008970:Molecular Weight; D010744:Phosphoric Monoester Hydrolases / Q000097:blood*; D011487:Protein Conformation
chemical_list: D007527:Isoenzymes; C022408:phosphoglycolate phosphatase; D010744:Phosphoric Monoester Hydrolases