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

TY - JOUR

T1 - Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition

AU - Rasmussen, Søren K.

AU - Klausen, Janne

AU - Hejgaard, Jørn

AU - Svensson, Birte

AU - Svendsen, Ib

PY - 1996/10/17

Y1 - 1996/10/17

N2 - 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.

AB - 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.

KW - Acetylated N-terminus

KW - Amino acid sequence

KW - CDNA

KW - Hordeum vulgare

KW - Protein Z

UR - http://www.scopus.com/inward/record.url?scp=0030591752&partnerID=8YFLogxK

U2 - 10.1016/S0167-4838(96)00115-X

DO - 10.1016/S0167-4838(96)00115-X

M3 - Journal article

C2 - 8917613

AN - SCOPUS:0030591752

SN - 1570-9639

VL - 1297

SP - 127

EP - 130

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

IS - 2

ER -