PMID: 2105083Jan 1, 1990Paper

Formation of cyclic imide-like structures upon the treatment of calmodulin and a calmodulin peptide with heat

Archives of Biochemistry and Biophysics
B L MartinD J Graves

Abstract

Protein cyclic imide is the putative intermediate in the formation of sites of carboxyl-methylation in eukaryotic proteins. Conditions known to induce the formation of a cyclic imide in model peptides have been applied to a protein, calmodulin. Heating of calmodulin in the dry state at 100 degrees C for 24 h after lyophilization from a pH 2.0 or pH 6.0 solution produces derivatives with altered chromatographic properties in anion-exchange HPLC. At pH 6.0, complete activity of calmodulin was retained. Analysis with Fourier transform infrared (FTIR)-photoacoustic spectroscopy demonstrated the presence of a new structure in the calmodulin molecule consistent with modification of carboxylic acid groups. The conversion of calmodulin is dependent upon the absence of Ca2+ (the presence of 1 mM ethylene glycol bis(beta-aminoethyl ether) N,N'-tetraacetic acid). A peptide analogous to the calcium binding regions of calmodulin, Asp-Lys-Asp-Gly-Asn-Gly-Thr-Ile-Thr-Thr-Lys-Glu, is also converted, upon heating, to chromatographically different forms in reversed-phase chromatography. This process is also dependent upon the absence of calcium. Sequence analysis of the peptide derivatives reveals a second amino terminus, implicating peptide bon...Continue Reading

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Citations

Jul 22, 2014·Journal of Pharmaceutical Sciences·Joshua J KlaeneZhaohui Sunny Zhou
Aug 20, 1990·FEBS Letters·P J GroenenW W de Jong
Dec 1, 1993·International Journal of Peptide and Protein Research·A M PistoriusW J De Grip

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