Amino acid sequence of an active fragment of potato proteinase inhibitor IIa.

Abstract:

:The complete amino acid sequence of an active fragment of potato proteinase inhibitor IIa has been established by the Edman degradation procedure and the carboxypeptidase technique. Sequence analyses were carried out on the reduced and carboxymethylated active fragment and its tryptic peptides. To aid in the alignment of some tryptic peptides, the partial sequences of two fragments obtained by selective tryptic cleavage of the reactive site peptide bond of inhibitor IIa at acidic pH, with subsequent reduction and carboxymethylation, were also analyzed. The active fragment consisted of 45 amino acid residues including 6 half-cystine residues. Degradation of the intact active fragment by subtilisin [EC 3.4.21.14.] at pH 6.5. yielded 3 cystine-containing peptides. Sequence analyses of these peptides revealed that the 3 disulfide linkages were located between Cys(10) and Cys(24), Cys(14) and Cys(35), and Cys(20) and Cys(43). The reactive site peptide bond of inhibitor IIa, a Lys-Ser bond, was located between positions 32 and 33 of the active fragment. The overall sequence of the active fragment was quite different from those of potato chymotrypsin inhibitor I (subunit A) and potato carboxypeptidase inhibitor.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Iwasaki T,Kiyohara T,Yoshikawa M

doi

10.1093/oxfordjournals.jbchem.a131081

keywords:

subject

Has Abstract

pub_date

1976-02-01 00:00:00

pages

381-91

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

79

pub_type

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