Abstract
Enzymatic methylation of arginine and lysine residues of several cytochromec and lysine residue of calmodulin always resulted in lowering of their respective isoelectric points (pI). Employing cytochromesc derived from various sources, we examined a possible relationship between the degree of amino acid sequence degeneracy and the magnitude of change in the pI values by enzymatic methylation, and found that there was no correlation between these two parameters. By constructing space-filling models of oligopeptide fragments adjacent to the potential methylation sites, we have noted that not all the methylatable residues are able to form hydrogen bonds prior to the methylation. Two preparations of yeast apocytochromec, one chemically prepared by removing heme from holocytochromec and the other by translating yeast iso-1-cytochromec mRNAin vitro, exhibited slightly higher Stokes radii than the homologous holocytochromec, indicating relatively “relaxed or open” conformation of the protein. However, when thein vitro synthesized methylated apocytochromec was compared with the unmethylated counter-part, the Stokes radius of the latter was found to be larger.
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Park, K.S., Frost, B.F., Lee, H.W. et al. Effect of enzymatic methylation of proteins on their isoelectric points. Arch. Pharm. Res. 12, 79–87 (1989). https://doi.org/10.1007/BF02857727
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DOI: https://doi.org/10.1007/BF02857727