Amino acid sequence of piguamerin, an antistasin-type protease inhibitor from the blood sucking leech Hirudo nipponia.
A serine-protease inhibitor of plasma kallikrein was screened and purified from a native Korean leech species, Hirudo nipponia. The peptide, named piguamerin, potently inhibited plasma and tissue kallikreins, and trypsin. Sequence analyses by automated Edman degradation revealed 48 amino acid residues and a molecular mass for the peptide of 5090 Da. Piguamerin is similar to antistasin-type inhibitors with the same spacing of ten cysteine residues, but shows differences from hirustasin, antistasin and ghilanten at the residues surrounding Arg27, which is a common P1 reactive residue for these inhibitors. The purified inhibitor modulated plasma clotting in tests of activated partial thromboplastin time at nanomolar concentrations. The serine-protease inhibitor of this leech may be involved in leech hematophagia.
Kim
D R
DR
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon.
Kang
K W
KW
D000595:Amino Acid Sequence; D000818:Animals; D000925:Anticoagulants / Q000737:chemistry* / Q000302:isolation & purification; D002851:Chromatography, High Pressure Liquid; D007447:Invertebrate Hormones / Q000737:chemistry* / Q000302:isolation & purification; D007865:Leeches / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D000925:Anticoagulants; D007447:Invertebrate Hormones; D015842:Serine Proteinase Inhibitors; C113614:piguamerin