Isolated rat liver mitochondrial membranes are found to contain tightly bound protein substrate(s) which can be phosphorylated in the presence of ATP by protein kinase(s) previously extracted with 0.7 M NaCl from the membranes themselves and by phosvitin kinase purified from liver cytosol. Such proteinkinase-dependent phosphorylation, which seems to be cyclic AMP-independent, involves the seryl and threonyl residues of the protein substrate(s). © 1975.
Endogenous proteinkinase-dependent phosphorylation of rat liver mitochondrial membranes
MORET, VITTORIO;CLARI, GIULIO;PINNA, LORENZO
1975
Abstract
Isolated rat liver mitochondrial membranes are found to contain tightly bound protein substrate(s) which can be phosphorylated in the presence of ATP by protein kinase(s) previously extracted with 0.7 M NaCl from the membranes themselves and by phosvitin kinase purified from liver cytosol. Such proteinkinase-dependent phosphorylation, which seems to be cyclic AMP-independent, involves the seryl and threonyl residues of the protein substrate(s). © 1975.
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