6533b7d8fe1ef96bd126af78
RESEARCH PRODUCT
Purification, isolation and characterization of a phosphoglycolate phosphatase isoenzyme from human erythrocytes.
Udo SchwuléraReinhard ZecherH. Uwe Wolfsubject
Trischemistry.chemical_classificationChromatographyErythrocytesHot TemperatureIsoelectric focusingProtein ConformationBiologyHydrogen-Ion ConcentrationBiochemistryIsozymePhosphoric Monoester HydrolasesMOPSIsoenzymesMolecular Weightchemistry.chemical_compoundKineticsIsoelectric pointEnzymechemistryBiochemistryHumansSpecific activityIsoelectric PointPhosphoglycolate phosphatasedescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1982-01-01 | The International journal of biochemistry |