Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes.
We have been able to separate protein carboxyl methyltransferase activity from human erythrocyte cytosol into two major fractions by DEAE-cellulose chromatography. These isozymes, designated I and II, are characterized by their isoelectric points of approximately 6.6 and 5.5 as determined by isoelectric focusing in polyacrylamide gels. The ratio of the isozymes (II/I) was found to range from 0.52 to 1.2 in blood samples from 14 individuals. We did not detect differences in this ratio between males and females. We also found no differences between freshly drawn and outdated blood samples. Both isozymes catalyzed the methylation of proteins such as ovalbumin as well as synthetic L-isoaspartyl-containing peptides.
Ota
I M
IM
Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.
Gilbert
J M
JM
Clarke
S
S
D000328:Adult; D000818:Animals; D004912:Erythrocytes / Q000201:enzymology*; D005260:Female; D006736:Horses; D006801:Humans; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007527:Isoenzymes / Q000097:blood*; D008297:Male; D008875:Middle Aged; D008970:Molecular Weight; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; D011496:Protein Methyltransferases / Q000097:blood*; D011817:Rabbits; D051381:Rats; D014101:Torpedo
D007527:Isoenzymes; D011496:Protein Methyltransferases; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase