Abstract
Polymyxin B, a cyclic peptide antibiotic, inhibits Ca2+-ATPase, p-nitrophenyl phosphatase and phosphorylase kinase activities associated with rabbit skeletal muscle sarcoplasmic reticulum membranes; 50% inhibition is induced by 100 μM, 130μM and 550 μM of polymyxin respectively. The fluorescence intensity of fluorescein isothiocyanate-labeled Ca2+-ATPase, decreases in the presence of polymyxin (50% of the total decrease at 70 μM polymyxin). On the other hand, the polypeptide inhibits calmodulin-dependent endogenous phosphorylation of 60 kDa, 20 kDa and 14 kDa membrane proteins, while an increase of calmodulin-dependent phosphorylation is observed in 132 kDa and 86 kDa proteins.
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Ktenas, T.B., Sotiroudis, T.G. & Evangelopoulos, A.E. Effects of polymyxin B on the sarcoplasmic reticulum membrane. Biosci Rep 9, 573–578 (1989). https://doi.org/10.1007/BF01119800
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DOI: https://doi.org/10.1007/BF01119800