Primary Structure of Hemorrhagic Protein, HR2a, Isolated from the Venom of Trimeresurus flavoviridis

The complete amino acid sequence and disulfide bridge location of HR2a, one of the hemorrhagic proteins isolated from the snake venom of Trimeresurus flavoviridis, have been determined by analysis of peptides derived from digests with cyanogen bromide, lysyl endopeptidase, trypsin, and Staphylococcu...

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Veröffentlicht in:	Journal of biochemistry (Tokyo) 1989-05, Vol.105 (5), p.847-853
Hauptverfasser:	Miyata, Toshiyuki, Takeya, Hiroyuki, Ozeki, Yasushi, Arakawa, Mitsue, Tokunaga, Fuminori, Iwanaga, Sadaaki, Omori-Satoh, Tamotsu
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Crotalid Venoms - analysis Disulfides - analysis Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Hydrolysis Miscellaneous Molecular Sequence Data Molecular Weight Peptides - analysis Peptides - isolation & purification Protein Conformation protein HR2a Proteins Serine Endopeptidases Sulfhydryl Compounds - analysis Trimeresurus flavoviridis Trypsin venom
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Zusammenfassung:	The complete amino acid sequence and disulfide bridge location of HR2a, one of the hemorrhagic proteins isolated from the snake venom of Trimeresurus flavoviridis, have been determined by analysis of peptides derived from digests with cyanogen bromide, lysyl endopeptidase, trypsin, and Staphylococcus aureus V8 protease. Peptides were purified by gel filtration followed by reversed-phase HPLC. HR2a has the amino-terminal sequence of
ISSN:	0021-924X 1756-2651
DOI:	10.1093/oxfordjournals.jbchem.a122756