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JBC, Vol. 251, Issue 4, 1009-1014, Feb, 1976
J. L. Brown and W. K. Roberts
Analysis of soluble Ehrlich ascites proteins by the Sanger procedure
revealed methionine, alanine, valine, and glycine as the major NH2-terminal
amino acids. The average monomer weights of these proteins calculated from
the yields of NH2-terminal amino acids was 144,000. In contrast, the
average monomer weight of Ehrlich ascites soluble proteins calculated from
the data obtained after electrophoresis in polyacrylamide gels containing
sodium dodecyl sulfate was 32,500. The explanation for the disparity in the
estimates of average monomer weight obtained by the procedures appears to
be that extensive blocking of alpha-NH2 groups by acetate occurs in these
proteins, i.e. of the acetate present in the acidic peptides isolated from
proteolytic digests of ascites proteins, 23.2 nmol/mg of protein appears to
originate from N-acetyl amino acids. These results suggest that
approximately 80% of the soluble proteins from Ehrlich ascites cells
contain acetate at their NH2-terminal residues. The extensive N-acetylation
of proteins does not appear to be limited to Ehrlich ascites cells and may
be characteristic of eukaryotic proteins.
Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nalpha-acetylated
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