Abstract
1. 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. 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. 3. The enzyme is composed of two subunits (mol. wt 35,000) which are identical and not connected by SS-bridges. 4. 4. At 4°C the isoenzyme is more stable in the pH range of 7–9 than at acid pH values. 5. 5. Incubation at 30 and 40°C for 4 hr does not affect the activity of the isoenzyme. 6. 6. It has a K m -value of 0.28 mM for phosphoglycolate (PG) as substrate.
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