title: [Isolation and some properties of protein inhibitor of trypsin from acorns of the oak tree].
abstract: Four protein fractions with trypsin-inhibiting activity have been isolated from acorns of oak tree (Quercus robur L.) by chromatography on DEAE-cellulose. Further their purification on trypsin-agarose column have demonstrated 12 peaks of activity. Every fraction corresponded to these peaks, left the column with Sephadex G-50 with the same volume of elution that corresponded to molecular weight of 16000 +/- 10% dalton. It was concluded that they have the same protein inhibitor. All the fractions proved to be steady to high-temperature denaturation, 8 M carbamide and 0.1% SDS, but preserved not more than 20% of activity under dithiothreitol effect. All they had specificity to trypsin only and were significantly less active to chymotrypsin, peptine and pronase.
authors.forename: A A
authors.initials: AA
authors.lastname: Medvedkov
authors.forename: A V
authors.initials: AV
authors.lastname: Ivashov
mesh_terms: D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D011489:Protein Denaturation; D012639:Seeds / Q000737:chemistry*; D014197:Trees; D014361:Trypsin Inhibitors / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D010940:Plant Proteins; D014361:Trypsin Inhibitors
vernacular_title: Vydelenie i nekotorye svoĭstva belkovogo ingibitora tripsina iz zheludeĭ duba chereshchatogo.