Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition

Research output: Contribution to journalJournal articleResearchpeer-review

  • Søren K. Rasmussen
  • Janne Klausen
  • Jørn Hejgaard
  • Birte Svensson
  • Ib Svendsen

The primary structure of barley grain serpin BSZ7 was deduced from a cDNA encoding 397 amino-acid residues, More than 70% of the residues were confirmed by sequencing peptide fragments. The N-terminus was identified as an acetylated Ala by using mass spectrometry coupled with amino-acid analysis. None of the four putative N-glycosylation sites were found to be glycosylated. The positional identity of BSZ7 with plant and mammalian serpins is 69-72% and 25-32%, respectively.

Original languageEnglish
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1297
Issue number2
Pages (from-to)127-130
Number of pages4
ISSN0167-4838
DOIs
Publication statusPublished - 1996
Externally publishedYes

    Research areas

  • Acetylated N-terminus, Amino acid sequence, CDNA, Hordeum vulgare, Protein Z

ID: 204470420