Quantitative analysis of dissociation of LDH by high pressure native PAGE

Autor:	Ryo Ishiguro, Keiichi Kameyama, Tomoya Miwa, Tetsuro Fujisawa
Rok vydání:	2019
Předmět:	Chromatography Chemistry Tetrameric protein Native Polyacrylamide Gel Electrophoresis Native page 010502 geochemistry & geophysics Condensed Matter Physics 01 natural sciences Dissociation (chemistry) chemistry.chemical_compound Electrophoresis Lactate dehydrogenase High pressure 0103 physical sciences 010306 general physics Quantitative analysis (chemistry) 0105 earth and related environmental sciences
Zdroj:	High Pressure Research. 39:218-224
ISSN:	1477-2299 0895-7959
Popis:	High pressure native polyacrylamide gel electrophoresis has been designed to visualize the dissociation/association process of protein complexes. This paper reports this methodology in more quantitative way by inspecting pressure dissociation of pig heart lactate dehydrogenase, a tetrameric protein, which was extensively investigated in spectroscopic methods. We observed the change of electrophoresis pattern with pressure up to 150 MPa. By optimizing the buffer system and careful image analysis of the stained gels, we quantified all the dissociates in the process of pressurization. We discussed the characteristics of our methodology by comparing the result with the previously reported.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::9bcaf72270eedeba0de5163dd1201ccd https://doi.org/10.1080/08957959.2018.1564822 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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