Abstract
A method is suggested to obtain and purify N-end fragments of A alpha-chain from bovine fibrinogen. To identify the N-end chain fragments the fluorescent properties of tryptophan and tyrosine composing them as well as hydrolysis by ancistron H, a thrombin-like enzyme of the snake venom, have been used for the first time.
MeSH terms
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Animals
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Cattle
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Chromatography, Liquid
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Fibrinogen / chemistry
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Fibrinogen / isolation & purification*
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Fibrinopeptide A / metabolism
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Fibrinopeptide B / metabolism
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Hydrolysis
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Serine Endopeptidases / chemistry
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Snake Venoms
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Spectrometry, Fluorescence
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Spectrophotometry, Ultraviolet
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Tryptophan / metabolism
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Tyrosine / metabolism
Substances
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Snake Venoms
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Fibrinopeptide A
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Fibrinopeptide B
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Tyrosine
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Tryptophan
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Fibrinogen
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Serine Endopeptidases
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ancistron N