A new trypsin inhibitor, bdellin for Korean leech (bdellin-KL), was is
olated from a blood sucking leech, Hirudo nipponia. It has a molecular
mass of 16156.4 Da and pi value of 4.0. The inhibitor was stable at a
range of pH 1.3 through 10.0 and temperatures ranging from 20 degrees
C to 90 degrees C. The bdellin-KL showed inhibition constants of 1.67
+/- 0.73 x 10(-9) M for trypsin and 1.76 +/- 1.29 x 10(-9) M for plas
min but a poor activity against chymotrypsin. Over 60 amino acid resid
ues of the N-terminal region showed a high similarity with those of th
e high-molecular mass bdellin B-3 (HMB), a European leech-derived tryp
sin-plasmin inhibitor. The first 10 residues that contained a P1 react
ive site of Lys and the spacing of six cysteines in the peptide are we
ll conserved for the two phylogenetically different species.