[Isolation and properties of trypsin inhibitor from the leaves of pedunculate oak].
Four protein fractions inhibiting trypsin are isolated from the English oak leaves by the method of chromatography on DEAE-cellulose. Three active fractions more are found in each of them after the affinity chromatography on trypsin-agarose. Each of 12 multiple forms in the calcium-free medium contains different sets of proteins and oligopeptides possessing rather high inhibiting activity. Ca2+ being introduced to the medium, all the multiple forms somewhat increase their activity, having one peak (Mm approximately 16.5 kDa) on the column with sephadex G-50. The inhibitor possesses high indices of denaturation stability and specificity to trypsin.
Medvedkov
A A
AA
Ivashov
A V
AV
D002118:Calcium / Q000502:physiology; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D008970:Molecular Weight; D011489:Protein Denaturation / Q000502:physiology; D014197:Trees; D014361:Trypsin Inhibitors / Q000302:isolation & purification*
D014361:Trypsin Inhibitors; D002118:Calcium
Vydelenie i nekotorye svoĭstva ingibitora tripsina iz list'ev duba chereshchatogo.