[Inhibition of cathepsin G and elastase from human granulocytes by multiple forms of the Bowman-Birk type of soy inhibitor].
A classical soybean inhibitor (Bowman-Birk inhibitor, BBI 2-IV) and two high molecular weight glycine-enriched inhibitors of the same type (3-II and 4-II) have been isolated, purified to homogeneity and characterized. All of the BBI isoforms have been found to effectively inhibit cathepsin G and human granulocyte elastase. The constants for leucocyte cathepsin G inhibition by classical BBI 2-IV (Ki = 1.2 x 10(-9) M) and high molecular mass BBI 3-II (Ki = 8.0 x 10(-8) M) as well as for leucocyte elastase inhibition by high molecular mass BBI 3-II (Ki = 1.1 x 10(-7) M) have been determined.
Larionova
N I
NI
Gladysheva
I P
IP
Tikhonova
T V
TV
Kazanskaia
N F
NF
D000596:Amino Acids / Q000032:analysis; D002403:Cathepsins / Q000037:antagonists & inhibitors*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*
D000596:Amino Acids; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D002403:Cathepsins; D010196:Pancreatic Elastase
Ingibirovanie katepsina G i élastazy granulotsitov cheloveka mnozhestvennymi formami soevogo ingibitora tipa Baumana-Birk.