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Open Access Green as soon as Postprint is submitted to ZB.
Amino acid sequence of yeast proteinase B inhibitor 1 comparison with inhibitor 2.
Biochem. Biophys. Res. Commun. 91, 1390-1398 (1979)
The amino acid sequence of proteinase B inhibitor 1 (IB1) from bakers' yeast has been established by automated Edman degradation up to position 42. A comparison with the sequence of proteinase B inhibitor 2 (IB2) revealed two differences: LEU-32 and GLU-34 in IB2 are replaced by VAL-32 and LYS-34 in IB1. Identity of the COOH-terminal region of IB1 with that of IB2 was proved by degradation with the carboxypeptidases A and Y. Furthermore, a chymotryptic peptide was isolated from each of the 74 residues containing inhibitors. The two fragments, ranging from position 42 to the COOH termini of the inhibitors, were found to be identical with respect to electrophoretical mobility, end groups, amino acid composition and peptide pattern after tryptic digestion. It is concluded, that the two inhibitor sequences are identical beyond position 42. IB1 and IB2 are isoinhibitors, because they are coded by different genes.
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Publication type
Article: Journal article
Document type
Scientific Article
Language
english
Publication Year
1979
HGF-reported in Year
0
ISSN (print) / ISBN
0006-291X
e-ISSN
1090-2104
Quellenangaben
Volume: 91,
Issue: 4,
Pages: 1390-1398
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Institut für Toxikologie und Biochemie
Scopus ID
0018639759
Erfassungsdatum
1979-12-31