Isolation and characterization of some proteinase inhibitors from Phaseolus vulgaris var. nanus.
Six proteinase inhibitors have been isolated from a crude inhibitor preparation from Phaseolus vulgaris var. nanus (bush bean: Borlotto) by gel chromatography and ion exchange chromatography. The isoelectric points of the inhibitors are between 4.35 and 5.65. The molecular weights of the inhibitors PVI-2, -3(1), -3(2), and -4 and between 8000 and 9500. The C-terminal and N-terminal amino acid residues and the amino acid compositions of these four inhibitors are given. The inhibitors PVI-1, -2, -3(1), -3(2), -4, and 5(1) all inhibit trypsin and with the exception of PVI-3(1) also alpha-chymotrypsin. PVI-3(1) inhibit elastase. The inhibitor mixture, PVI-G, exhibits a weak inhibition of some microbial serine proteinases. Some other endopeptidases and exopeptidases tested are not inhibited. Crude inhibitor preparations from P. coccineus and Pisum sativum show the same behaviour.
D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D007887:Fabaceae; D010944:Plants / Q000032:analysis*; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D014361:Trypsin Inhibitors / Q000494:pharmacology
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin