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

Søren K Rasmussen, Janne Klausen, Jørn Hejgaard, Birte Svensson, Ib Svendsen

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    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
    Journal BBA - Protein Structure and Molecular Enzymology
    Volume1297
    Issue number2
    Pages (from-to)127-130
    ISSN0167-4838
    DOIs
    Publication statusPublished - 1996

    Keywords

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

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