SDS-binding assay based on tyrosine fluorescence as a tool to determine binding properties of human serum albumin in blood plasmaтезисы доклада
Информация о цитировании статьи получена из
Web of Science,
Scopus
Дата последнего поиска статьи во внешних источниках: 17 ноября 2016 г.
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Авторы:
Zhdanova N.,
Shirshin E.,
Fadeev V.,
Priezzhev A.
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Сборник:
Saratov Fall Meeting 2015
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Серия:
Proc. of SPIE
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Том:
9917
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Тезисы
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Год издания:
2016
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Место издания:
SPIE Proc. SPIE Bellingham, Washington
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Первая страница:
991713
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DOI:
10.1117/12.2229850
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Аннотация:
Among all plasma proteins human serum albumin (HSA) is the most studied one as it is the main transport protein and can bind a wide variety of ligands especially fatty acids (FAs). The concentration of FAs bound to HSA in human blood plasma differs by three times under abnormal conditions (fasting, physical exercises or in case of social important diseases). In the present study a surfactant sodium dodecyl sulfate (SDS) was used to simulate FAs binding to HSA. It was shown that the increase of Tyr fluorescence of human blood plasma due to SDS addition can be completely explained by HSA-SDS complex formation. Binding parameters of SDS-HSA complex (average number of sites and apparent constant of complex formation) were determined from titration curves based on tyrosine (Tyr) fluorescence. © (2016) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
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Добавил в систему:
Приезжев Александр Васильевич