Hi Manfred,
There was a paper by J.L. Brown and W.K. Roberts (1976),
J.Biol.Chem. 251:1009-1014, in which they found that approximately 80% of
the soluble proteins in Ehrlich ascites cells (and probably other
eukaryotic cells) are acetylated at their N-terminal residues.
Another paper which may be relevant is a survey of 250 proteins
with N-terminal acetylation by Persson et al. (Eur.J.Biochem. (1985),
152:523-527). They looked at the N-terminal sequence of 105 of these
proteins and found that the most frequently acetylated residue was serine
(43/105), followed by alanine (33/105).
You may be interested in a method which is available for
selectively removing the acetyl group from an N-terminal N-acetylserine (or
N-acetylthreonine). This method allows the blocked protein to be sequenced
by Edman degradation. (D. Wellner et al.(1990), Proc.Nat.Acad.Sci.USA
87:1947-1949).
Best wishes,
Daniel
Daniel Wellner, Ph.D.
Department of Biochemistry
Weill Medical College of Cornell University
New York, NY 10021
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