PMID: 6427007May 21, 1984Paper

Acetyl-blocked N-terminal structures of sorbitol and aldehyde dehydrogenases

FEBS Letters
T FairwellH Jörnvall


Two new dehydrogenase structures, the 354-residue polypeptide chain of sorbitol dehydrogenase (from sheep liver) and the 500-residue polypeptide chain of cytoplasmic aldehyde dehydrogenase (from human liver), have blocked N-termini. The N-terminal peptides were purified by reverse-phase high-performance liquid chromatography and submitted to mass spectrometry after derivatization. They were also analyzed by dipeptidyl carboxypeptidase digestion, utilizing gas chromatography-mass spectrometry for dipeptide identifications. Results are consistent and establish that sorbitol dehydrogenase has N-terminal acetylalanine and aldehyde dehydrogenase N-terminal acetylserine in amino acid sequences that are compatible with estimates from chemical analyses. The two N-terminal residues found are typical of acetylated proteins in general, extend the group of known acetylated dehydrogenases, and show that these intracellular proteins are frequently N-terminally acetylated.


Mar 1, 1971·Archives of Biochemistry and Biophysics·M C BrummelL D Stegink
Oct 20, 1970·Biochimica Et Biophysica Acta·B M SanbornC S Vestling
Jan 1, 1983·Pharmacology, Biochemistry, and Behavior·H JörnvallJ Jeffery
Nov 2, 1983·European Journal of Biochemistry·H P DriessenH Bloemendal
Jul 15, 1983·European Journal of Biochemistry·H von Bahr-LindströmH Jörnvall

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