Primary structures of proteinase inhibitors from Phaseolus vulgaris var. nanus (cv. Borlotto).
The primary structures of two trypsin-chymotrypsin inhibitors from Phaseolus vulgaris var. nanus (bush bean, cv. Borlotto), PVI-3(2) und PVI-4, were derived from automated Edman degradation data, amino acid composition and manual Edman degradation results of enzymatic fragments and homology with other Bowman-Birk type proteinase inhibitors. The highest degrees of homology were observed between PVI-3(2) or PVI-4 and the trypsin-chymotrypsin inhibitors from lima beans (LBI I, IV and IV', 86%), black-eyed peas (BTCI, 81%), and, in part, adzuki beans (ABI I, II and II', 74-77%). Similarly, the primary structure of the trypsin-elastase inhibitor from the same source, PVI-3(1), was deduced which showed highest homology with that of the trypsin-elastase inhibitor GBI II from garden beans (92%), followed by GBI II' from garden beans (86%) and C-II from soybeans (71%). In contrast, homology between PVI-3(2) and PVI-4 on the one hand and PVI-3(1) on the other was relatively low (61%).
Deutsche Forschungsanstalt für Lebensmittelchemie, Technische Universität München, Garching, Germany.
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D007887:Fabaceae / Q000737:chemistry* / Q000201:enzymology; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D010940:Plant Proteins / Q000737:chemistry*; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000737:chemistry; D017385:Sequence Homology; D014361:Trypsin Inhibitors / Q000737:chemistry*
D000596:Amino Acids; C081191:PIV-4 protein, Phaseolus vulgaris; C081192:PVI-3(1) protein, Phaseolus vulgaris; C081190:PVI-3(2) protein, Phaseolus vulgaris; D010940:Plant Proteins; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin; D010196:Pancreatic Elastase