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- W177724453 abstract "This chapter describes the role of calmodulin as a substrate and activator of protein methylation. Calmodulin from most species contains a single residue of trimethyllysine. Troponin C, which shares considerable amino acid sequence homology but not biological activity with calmodulin is not methylated. This has given rise to speculation that N-methylation may contribute to the biological activities of calmodulin. An assay for the enzyme that methylates calmodulin (calmodulin N-methyltransferase, CLNMT) shows that N-methylation selectively modifies the biological activities of calmodulin, and that calmodulin N-methyltransferase is specific for calmodulin and is subject to physiological regulation. It is found that when rat brain cytosol is incubated with [methyl-3H]-AdoMet and methylated proteins are fractionated, Calmodulin is found to be the major methyl acceptor. The addition of exogenous mammalian calmodulin inhibits calmodulin methylation. This finding implies that brain contains some des(methyl)calmodulin. Calmodulin from dictyostelium discoideum contains nonmethylated calmodulin and this protein was used as the substrate for a radiometric assay. It is found that in hepatoma, neonatal liver and brain, and regenerating liver CLNMT is markedly elevated." @default.
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- W177724453 date "1987-01-01" @default.
- W177724453 modified "2023-09-27" @default.
- W177724453 title "CALMODULIN AS A SUBSTRATE AND ACTIVATOR OF PROTEIN METHYLATION11Supported by NIH Grants NS 11652 and H# 03552." @default.
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- W177724453 doi "https://doi.org/10.1016/b978-0-12-521040-9.50090-5" @default.
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