Výsledky vyhledávání - "V. A. Belitser"

[Modification of fibrin assembly as a method for studying the mechanism of this process]

Publikováno v: Ukrains'kyi biokhimichnyi zhurnal. 47(5)

A study of monomeric fibrin assembly--the process at which the ordered fibres are formed and at the definite moment there arises an elastic three-dimension net (coagulation occurs) made it possible to establish the following. Fibrinogen and high-mole

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ae9732779f13c70723131e69626520f6
https://pubmed.ncbi.nlm.nih.gov/1202701

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[Interaction of fibrinogen with two forms of fibrin differing in the degree of activation by thrombin]

Autor: V A, Belitser, E V, Lugovskoĭ, T P, Ugarova, S G, Derzskaia

Publikováno v: Biokhimiia (Moscow, Russia). 50(8)

The inhibitory effect of fibrinogen in the clotting of two fibrin monomer species--f-desAA and f-desAABB--was studied. The concentration dependence of this effect for two fibrin forms was found to be of the same character. This fact indicates that th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1a3e124a871417781364bb5f663f8226
https://pubmed.ncbi.nlm.nih.gov/4074798

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[Determination of fibrin and fibrinogen split products by their anticoagulant activity]

Autor: V A, Belitser, T V, Varetskaia, S N, Tsynkalovskaia, L A, Tsariuk, L I, Shevchenko

Publikováno v: Ukrains'kyi biokhimichnyi zhurnal. 48(4)

A new diagnostic method to determine fibrinogen and fibrin splitting products is based on the fact that high-molecular fragments acting as specific inhibitors of fibrin self-assembly compose these products. Fibrinogen and fibrin splitting products ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::12170cac0f2ce65ba9e36950461cd9db
https://pubmed.ncbi.nlm.nih.gov/982623

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[Fibrinogen and fibrin monomer conformation changes dependent of pH magnitude]

Autor: A P, Demchenko, V L, Zima, T F, Galanova, V A, Belitser

Publikováno v: Molekuliarnaia biologiia. 10(2)

Conformational states of fibrinogen and fibrin monomer were studied by methods of differential and solvent-perturbation spectrophotometry and ultraviolet fluorescence at about neutral pH (6.5) and in the region of lower pH, 3.2 to 4.0. To prevent rep

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::58ec72df0caca51df569d0b497c33805
https://pubmed.ncbi.nlm.nih.gov/7745

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[Interaction of an analog of the E1 site of tetrapeptide Gly-Pro-Arg-Pro with the D1 site of two forms of monomeric fibrin]

Autor: T P, Ugarova, V P, Romanova, V A, Belitser

Publikováno v: Ukrainskii biokhimicheskii zhurnal (1. 58(2)

Two monomeric fibrin forms differing in a set of polymerization sites (fibrin desAA and fibrin-desAABB) are inhibited to a different extent by tetrapeptide Gly-Pro-Arg-Pro which simulates a moiety of polymerization site E1. The lesser sensitivity of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b2ff076034e4cc4bf8ae7c93ae3cbd5b
https://pubmed.ncbi.nlm.nih.gov/3705201

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