CHARACTERIZATION OF ACTIVE-SITE OF A NEW TRYPSIN AND CHYMOTRYPSIN INHIBITOR FROM POTATO-TUBER

Authors
REVINA TA VALUEVA TA ERMOLOVA NV MOSOLOV VV
Citation
Ta. Revina et al., CHARACTERIZATION OF ACTIVE-SITE OF A NEW TRYPSIN AND CHYMOTRYPSIN INHIBITOR FROM POTATO-TUBER, Biochemistry, 61(1), 1996, pp. 93-96
Citations number
17
Categorie Soggetti
Biology
Journal title
Biochemistry → ACNP
ISSN journal
00062979
Volume
61
Issue
1
Year of publication
1996
Pages
93 - 96
Database
ISI
SICI code
0006-2979(1996)61:1<93:COAOAN>2.0.ZU;2-W
Abstract
We studied the effect of modification of lysine, arginine, and methion ine residues in the proteinase inhibitor (a 17-kD protein) previously isolated from potato tuber on its inhibitor activity. Our data suggest that the protein has two independent active sites, for trypsin and fo r chymotrypsin. We conclude that the active sites for trypsin and chym otrypsin have lysine and methionine in the pi position, respectively.