[Association of rabbit skeletal muscle phosphorylase kinase with sarcoplasmic reticulum membranes].
The binding of phosphorylase kinase to sarcoplasmic reticulum has been studied using gel chromatography. The presence of Ca2+, Mg2+ and glycogen was found to be necessary for the maximal binding. The phosphorylase kinase adsorbed on sarcoplasmic reticulum is capable of phosphorylating exogenous phosphorylase b. Phosphorylase kinase was shown to take no part in the phosphorylation of sarcoplasmic reticulum proteins. Exogenous calmodulin initiates the incorporation of [gamma-32P] of ATP into sarcoplasmic reticulum proteins. The data obtained point to a possibility that another Ca(2+)-calmodulin-dependent protein kinase may participate in the phosphorylation of sarcoplasmic proteins.
Zemskova
M A
MA
Shur
S A
SA
Skolysheva
L K
LK
Vul'fson
P L
PL
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002850:Chromatography, Gel; D006003:Glycogen / Q000378:metabolism; D008274:Magnesium / Q000378:metabolism; D018482:Muscle, Skeletal / Q000201:enzymology*; D010764:Phosphorylase Kinase / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D006003:Glycogen; D010764:Phosphorylase Kinase; D008274:Magnesium; D002118:Calcium