The serine proteinase inhibitor (PSPI-51) isolated from potato tubers (Sola
num tuberosum L,) comprises two protein species with pi 5.2 and 6.3, denote
d as PSPI-21-5.2 and PSPI-21-6.3, respectively. They were separated by anio
n exchange chromatography on a Mono Q FPLC column. Both species tightly inh
ibit human leukocyte elastase, whereas their interaction with trypsin and c
hymotrypsin is substantially weaker. The sequences of both PSPI-21-5.2 and
PSPI-21-6.3 were determined by analysis of overlapping peptides obtained fr
om the oxidized or reduced and S-pyridylethylated proteins after digestion
with trypsin or pepsin, Both species of PSPI-21 are composed of two chains,
named chains A and B, which are linked by a disulfide bridge between Cys(1
46) and Cys(157). The other disulfide bridge is located within the A chains
between Cys(48) and Cys(97). The amino acid sequences of the large A chain
s of the two forms, consisting of 150 amino acids residues each, differ in
a single residue at position 52. The small chains B, containing 37 and 36 r
esidues in PSPI-21-6.3 and PSPI-21-5.2, respectively, have nine different r
esidues. The entire amino acid sequences of the two inhibitors show a high
degree of homology to the other Kunitz-type proteinase inhibitors from plan
ts.