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.
- Acetylated N-terminus
- Amino acid sequence
- Protein Z
- Hordeum vulgare
Rasmussen, S. K., Klausen, J., Hejgaard, J., Svensson, B., & Svendsen, I. (1996). Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition. BBA - Protein Structure and Molecular Enzymology, 1297(2), 127-130. https://doi.org/10.1016/S0167-4838(96)00115-X