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 conta...

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Veröffentlicht in:	FEBS letters 1991-12, Vol.294 (1), p.141-143
Hauptverfasser:	Siddiqi, Abdur Rehman, Zaidi, Zafar H., Jörnvall, Hans
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences C-terminal extension Chromatography, High Pressure Liquid - methods Contact site Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Homology Hydrolases Molecular Sequence Data Sequence Homology, Nucleic Acid Serpentes Snakes Trypsin inhibitor Trypsin Inhibitor, Kunitz Soybean - chemistry Trypsin Inhibitors - chemistry Trypsin Inhibitors - isolation & purification Viper Venoms
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Beschreibung
Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(91)81361-B