[Isolation and some properties of protein inhibitor of trypsin from acorns of the oak tree].
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.
Medvedkov
A A
AA
Ivashov
A V
AV
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*
D010940:Plant Proteins; D014361:Trypsin Inhibitors
Vydelenie i nekotorye svoĭstva belkovogo ingibitora tripsina iz zheludeĭ duba chereshchatogo.