Cam. Sampaio et al., PLANT SERINE PROTEINASE-INHIBITORS - STRUCTURE AND BIOCHEMICAL APPLICATIONS ON PLASMA KALLIKREIN AND RELATED ENZYMES, Immunopharmacology, 32(1-3), 1996, pp. 62-66
The action of two Bowman-Birk and several plant Kunitz-type inhibitors
were studied on trypsin, chymotrypsin, plasma kallikrein and factor X
II. The primary structure of some of them was completely defined. The
results showed that the Bowman-Birk type inhibitors, although potent i
nhibitors for trypsin (K-i in the range of 1-2 nM), are not able to in
hibit plasma kallikrein, Factor XII (K-i = 1.4 mu M) and chymotrypsin
(K-i = 5.0 nM) are inhibited by Torresea cearensis trypsin inhibitor (
TcTI) but not by Dioclea glabra trypsin inhibitor (DgTI). Both inhibit
ors reactive site regions are highly homologous, and the amino acid re
sidues in P1 position are the same, Lys and His; major differences are
in the charge of the C-terminal portion of the molecules, The studied
Kunitz-type inhibitors were all able to inhibit plasma kallikrein (Ki
between 4 and 80 nM), with the exception of Schizolobium parahyba chy
motrypsin inhibitor (SpCI), that is specific for chymotrypsin. All Kun
itz-type inhibitors inactivate chymotrypsin, but with a dissociation c
onstant in the range of 0.1 to 0.6 mu M Factor XIIf is inhibited with
K-i in the range of 0.1 mu M. Bauhinia bauhinioides trypsin inhibitor
(BbTI) did not promote factor XIIf inhibition. The Kunitz-type inhibit
ors are a highly homologous, sharing 60% identity in the N-terminal po
rtion of the loop containing the reactive site, and 28.6% identity in
the C-terminal portion of the same loop.