Inside-out vesicles from erythrocyte membrane were phosphorylated in the presence of γ-32P-ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase increased the 32P-labelling of membrane proteins and polyphosphoinositides in some red blood cell membrane preparations (RBC membrane, type I) while in the majority of membrane preparations the effect of the exogeneous catalytic subunit was insignificant (RBC membrane, type II). The phosphorylation of type II RBC membrane preparations seemed to be stimulated by the catalytic subunit of endogenous protein kinase, since the 32P-incorporation into polyphosphoinositides and proteins was decreased by the specific heat stable inhibitor protein of the protein kinase.
|Journal||Biomedica Biochimica Acta|
|Publication status||Published - Dec 1 1983|
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