Fast atom bombardment mass spectrometry and chemical analysis in determinations of acyl-blocked protein structures

Börje Egestad, Mats Estonius, Olle Danielsson, Bengt Persson, Ella Cederlund, Rudolf Kaiser, Barton Holmquist, Bert Vallee, Xavier Parés, Jonathan Jefferey, Hans Jörnvall

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14 Citations (Scopus)

Abstract

Peptide generation and fast atom bombardment mass spectrometry in combination with conventional chemical analysis was used to identify the blocking group and establish the N-terminal structure of six different proteins at the nanomole level. In this manner, the first terminal structures of three non-mammalian alcohol dehydrogenases were determined, demonstrating the presence of N-terminal acetylation in these piscine, amphibian, and avian enzymes. Similarly, two different yeast glucose-6-phosphate dehydrogenases and a minor variant of a human alcohol dehydrogenase were found to be acetylated. The exact end location of C-terminal structures was also established. Together, the analyses permit the definition of terminal regions and blocking groups, thus facilitating the delineation of remaining structures. © 1990.
Original languageEnglish
Pages (from-to)194-196
JournalFEBS Letters
Volume269
Issue number1
DOIs
Publication statusPublished - 20 Aug 1990

Keywords

  • Blocked peptide
  • C-terminal determination
  • Fast atom bombardment
  • Mass spectrometry
  • N-terminal acetylation

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