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RESEARCH PRODUCT
Phosphotransferase properties of human erythrocyte phosphoglycolate phosphatase.
H. Jochen SchäferH. Uwe WolfReinhard Zechersubject
ErythrocytesStereochemistryButanolMethanolPhosphotransferasesFructosePhosphateBiochemistryPhosphoric Monoester HydrolasesLactic acidSubstrate SpecificityPhosphotransferasePropanolNitrophenolschemistry.chemical_compoundOrganophosphorus CompoundschemistryBiochemistryAlcoholsTransferaseHumansPhosphoglycolate phosphatasedescription
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 glucose and fructose, and is even inhibited by 250 mM of lactose and lactic acid to 67 and 55%, respectively. 5. 5. Using p -nitrophenyl-[ 32 P]-phosphate ( p -NP[ 32 P]P). the direct transfer of phosphate from donor to acceptor could be demonstrated.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1982-01-01 | The International journal of biochemistry |