0000000000866464

AUTHOR

H. Jochen Schäfer

showing 2 related works from this author

The inhibition of Ca2+-ATPases of human erythrocyte membranes by covalent binding of ATP derivatives.

1982

AzidesErythrocytesChemistryUltraviolet RaysGeneral NeuroscienceErythrocyte MembraneCovalent bindingBiological Transport ActiveCa2 atpasesCalcium-Transporting ATPasesGeneral Biochemistry Genetics and Molecular BiologyKineticsMembraneAdenosine TriphosphateHistory and Philosophy of ScienceBiophysicsHumansEthenoadenosine TriphosphateProtein BindingAnnals of the New York Academy of Sciences
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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…

ErythrocytesStereochemistryButanolMethanolPhosphotransferasesFructosePhosphateBiochemistryPhosphoric Monoester HydrolasesLactic acidSubstrate SpecificityPhosphotransferasePropanolNitrophenolschemistry.chemical_compoundOrganophosphorus CompoundschemistryBiochemistryAlcoholsTransferaseHumansPhosphoglycolate phosphataseThe International journal of biochemistry
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