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

Phosphotransferase properties of human erythrocyte phosphoglycolate phosphatase.

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…