Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition.
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.
Rasmussen
S K
SK
Environmental Science and Technology Department, Risø National Laboratory, Roskilde, Denmark. soren.rasmussen@risoe.dk
Klausen
J
J
Hejgaard
J
J
Svensson
B
B
Svendsen
I
I
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D006031:Glycosylation; D001467:Hordeum / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D011994:Recombinant Proteins; D016415:Sequence Alignment; D017421:Sequence Analysis; D015843:Serpins / Q000737:chemistry*; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D010940:Plant Proteins; D011994:Recombinant Proteins; D015843:Serpins; D002918:Chymotrypsin; D014357:Trypsin