Isolation and identification of N-terminal fragments of the A-alpha chain of bovine fibrinogen

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 us...

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Bibliographic Details
Published inUkrainskij biohimičeskij žurnal Vol. 63; no. 2; p. 3
Main Authors Pekhnik, I V, Kheĭlomskiĭ, A B, Chikurova, E V
Format Journal Article
LanguageRussian
Published Ukraine 01.03.1991
Subjects
Animals
Cattle
Chromatography, Liquid
Fibrinogen - chemistry
Fibrinogen - isolation & purification
Fibrinopeptide A - metabolism
Fibrinopeptide B - metabolism
Hydrolysis
Serine Endopeptidases - chemistry
Snake Venoms
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Tryptophan - metabolism
Tyrosine - metabolism
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Summary: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.
ISSN:0201-8470