Výsledky vyhledávání - "S V, Litvinovich"

[Study on secondary structure and properties of alpha- and gamma-forms of human thrombin]

Autor: L P, Shvachko, S V, Litvinovich, V K, Kibirev

Publikováno v: Ukrains'kyi biokhimichnyi zhurnal (1999 ). 78(1)

Secondary structure and enzymatic properties of human a-thrombin and its gamma-form (obtaining during autolysis of the native enzyme) have been studied by differential scanning calorimetry (DSC) and circular dichroism (CD). According to DSC-data both

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::51548c3aa716b9ce81a71682afda9e85
https://pubmed.ncbi.nlm.nih.gov/17147270

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The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis

Autor: H, Tran, A, Tanaka, S V, Litvinovich, L V, Medved, C C, Haudenschild, W S, Argraves

Publikováno v: The Journal of biological chemistry. 270(33)

The fibulins are an emerging family of extracellular matrix and blood proteins presently having two members designated fibulin-1 and -2. Fibulin-1 is the predominant fibulin in blood, present at a concentration of 30-40 micrograms/ml (approximately 1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::29fb16285fc0ac55a1f02b298aa1f0e3
https://pubmed.ncbi.nlm.nih.gov/7642629

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Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded

Autor: S V, Litvinovich, D K, Strickland, L V, Medved, K C, Ingham

Publikováno v: Journal of molecular biology. 217(3)

The gelatin-binding region of fibronectin is isolated easily as a stable and functional 42 kDa fragment containing four type I "finger" modules and two type II "kringle-like" modules arranged in the order I6-II1-II2-I7-I8-I9. This fragment exhibits a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5f1d03d73537a59a736e624c39f9c9f4
https://pubmed.ncbi.nlm.nih.gov/1994038

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[A model of proteolysis of the fragment DH (95 kD) of the fibrinogen molecule]

Autor: S V, Litvinovich, L V, Medved'

Publikováno v: Molekuliarnaia biologiia. 22(4)

A detailed analysis of further proteolytic degradation of fibrinogen fragment DH (Mr 95 kDa) was performed. Two new proteolytic fragments DLA and DL derived from DH-fragment have been purified and analyzed. The results obtained allow to propose a gen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bfd45174c4e49852c6d80e0186427d89
https://pubmed.ncbi.nlm.nih.gov/3054505

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