Primary Structure of a Coagulant Enzyme, Bilineobin, from Agkistrodon bilineatus Venom

The amino acid sequence and disulfide bridge location of the coagulant enzyme, named bilineobin, isolated from the venom of Agkistrodon bilineatus was determined by Edman sequencing of the peptides derived from digests with cyanogen bromide, clostripain, Staphylococcus aureus V8 protease, trypsin, a...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1995-04, Vol.318 (1), p.89-96
Hauptverfasser:	Nikai, T., Ohara, A., Komori, Y., Fox, J.W., Sugihara, H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Agkistrodon - genetics Agkistrodon - metabolism Amino Acid Sequence Amino Acids - analysis Animals Carbohydrates - analysis Crotalid Venoms - chemistry Crotalid Venoms - genetics Crotalid Venoms - isolation & purification Cyanogen Bromide Cysteine Endopeptidases Disulfides - chemistry Enzyme Stability Fibrinogen - metabolism Humans In Vitro Techniques Isoelectric Point Molecular Sequence Data Molecular Structure Molecular Weight Neuraminidase - pharmacology Peptide Fragments - isolation & purification Rabbits Sequence Homology, Amino Acid Serine Endopeptidases - chemistry Serine Endopeptidases - genetics Serine Endopeptidases - isolation & purification Species Specificity Substrate Specificity
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