The state of phosphorylation in vivo of membrane-bound phosphoproteins in rat brain.

ABSTRACT: The alkali-labile P content of membrane protein prepared from rapidly frozen rat brain was measured, CuSO(4) being used to inhibit protein phosphatase activity during subcellular fractionation. The P content of the membrane fraction was significantly increased (+12%) over the control value by incubation of homogenates with ATP before fractionation. This suggests that the membrane protein in rat brain is normally only partially phosphorylated.

SUBMITTER: Weller M 

PROVIDER: S-EPMC1177709 | biostudies-other | 1973 Jun

REPOSITORIES: biostudies-other