Abstract:
:Glycogen phosphorylase b at concentrations close to those found in skeletal muscle interacts with sarcoplasmic reticulum membranes, but not with liposomes made of lipids extracted from these membranes, and is inhibited upon binding to the membrane. The interaction of glycogen phosphorylase with the sarcoplasmic reticulum membrane is modulated by phosphorylation, for the a form of this enzyme shows a K0.5 of interaction about 10-fold lower than the b form. Upon association to the membrane the fluorescence properties of the coenzyme of glycogen phosphorylase, pyridoxal-5'-phosphate, are strongly altered, for the fluorescence at 535 nm is partially quenched and the fluorescence at 415-420 nm increases. Using fluorescein labeled sarcoplasmic reticulum membranes we have found that the average conformation of the Ca2+ + Mg(2+)-ATPase is also altered on binding of phosphorylase b. In conclusion, the results reported in this paper suggest that glycogen phosphorylase and Ca2+ + Mg(2+)-ATPase directly interact under experimental conditions similar to those found in the sarcoplasm, and that this interaction is modulated by phosphorylation of the phosphorylase.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Cuenda A,Centeno F,Gutierrez-Merino Cdoi
10.1016/0014-5793(91)80606-4subject
Has Abstractpub_date
1991-06-03 00:00:00pages
273-6issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(91)80606-4journal_volume
283pub_type
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