title: [Isolation and properties of trypsin isoinhibitors from kidney beans].
abstract: Two isoinhibitors (II and III-B) have been isolated from kidney bean (Phaseolus vulgaris L.) in a highly purified state. Both were active against trypsin and chymotrypsin to the same extent. Their amino acid composition is characterized by a high content of half-cystine, aspartic acid (or asparagine) and serine, by the absence of valine, methionine and tryptophan. Glycine and serine were N-terminal in II and III-B respectively. Both isoinhibitors have C-terminal leucine.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D010944:Plants / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000302:isolation & purification
chemical_list: D000596:Amino Acids; D014361:Trypsin Inhibitors; D002918:Chymotrypsin
vernacular_title: Vydelenie i svoistva izoingibitorov tripsina iz fasoli.