[Isolation and characteristics of a new trypsin and chymotrypsin inhibitor from potato tubers].
A novel trypsin and chymotrypsin inhibitor has been isolated from potato (Solanum tuberosum L.) tubers. The isolation procedure included ammonium sulfate precipitation, gel-chromatography on Sephadex G-75 and ion-exchange chromatography on DEAE-cellulose. The inhibitor interacts with trypsin and chymotrypsin at a molar ratio of 1:1. The substrate-dependent dissociation of the enzyme-inhibitor complexes is observed. The inhibitor displays no activity towards subtilisin and pancreatic elastase. The ability of the inhibitor to form a ternary complex containing simultaneously both trypsin and chymotrypsin molecules testifies to the presence of two independent reactive sites for these enzymes.
Revina
T A
TA
Valueva
T A
TA
Ermolova
N V
NV
Kladnitskaia
G V
GV
Mosolov
V V
VV
D000595:Amino Acid Sequence; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D014361:Trypsin Inhibitors / Q000302:isolation & purification* / Q000378:metabolism
D014361:Trypsin Inhibitors; D002918:Chymotrypsin