Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom.
A Kunitz-type trypsin inhibitor was purified from Leaf-nosed viper venom and the primary structure determined by peptide analysis. In relation to other trypsin inhibitors, the protein has an extended C-terminal segment and a distinct pattern of residue alterations at the functionally important contact sites with proteases.
Siddiqi
A R
AR
Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
Zaidi
Z H
ZH
Jörnvall
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D012911:Snakes; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D014757:Viper Venoms
D014361:Trypsin Inhibitors; D014757:Viper Venoms; D014360:Trypsin Inhibitor, Kunitz Soybean