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  • Title: Enzyme transfer of phosphate from adenosine triphosphate to protein-bound serine residues in cerebral microsomes.
    Author: Rodnight R, Lavin BE.
    Journal: Biochem J; 1966 Nov; 101(2):495-501. PubMed ID: 4226015.
    Abstract:
    1. Microsomes from guinea-pig brain grey matter were incubated with [(32)P]ATP at 3mm concentration and the phosphate bound to the acid-washed, lipid-free residue was determined. 2. The binding process was Mg(2+)-dependent and resulted in the transfer of about 1-2 mmumoles of phosphate/mg. of protein/min. Under the conditions used univalent cations (Na(+),K(+) and Li(+)) inhibited the binding. 3. An unspecified proportion of this bound phosphate could be recovered in protein-derived phosphorylserine. The yield of labelled phosphorylserine was also decreased by univalent cations. 4. The bound phosphate formed with 3mm-MgATP was stable; addition of Na(+) or K(+) ions to the already labelled preparation had no effect on the bound phosphate level. 5. Bound phosphate was also formed when a solubilized fraction of the microsomes was incubated with ATP; univalent cations also inhibited this process. 6. p-Chloromercuribenzoate reduced the binding by about 25%; the inhibition was restored by cysteine.
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