title: [Isolation and characteristics of a new trypsin and chymotrypsin inhibitor from potato tubers].
abstract: 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.
authors.forename: T A
authors.initials: TA
authors.lastname: Revina
authors.forename: T A
authors.initials: TA
authors.lastname: Valueva
authors.forename: N V
authors.initials: NV
authors.lastname: Ermolova
authors.forename: G V
authors.initials: GV
authors.lastname: Kladnitskaia
authors.forename: V V
authors.initials: VV
authors.lastname: Mosolov
mesh_terms: 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
chemical_list: D014361:Trypsin Inhibitors; D002918:Chymotrypsin