Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition
Research output: Contribution to journal › Journal article › Research › peer-review
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 language | English |
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Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
Volume | 1297 |
Issue number | 2 |
Pages (from-to) | 127-130 |
Number of pages | 4 |
ISSN | 0167-4838 |
DOIs | |
Publication status | Published - 1996 |
Externally published | Yes |
- Acetylated N-terminus, Amino acid sequence, CDNA, Hordeum vulgare, Protein Z
Research areas
ID: 204470420