Analysis of oligomeric transition of silkworm small heat shock protein sHSP20.8 using high hydrostatic pressure native PAGE

Autor:	Keiichi Kameyama, Toshifumi Ueda, Tetsuro Fujisawa, Yoichi Aso, Ryo Ishiguro
Rok vydání:	2013
Předmět:	Transition (genetics) biology Hydrostatic pressure Native Polyacrylamide Gel Electrophoresis Condensed Matter Physics biology.organism_classification Oligomer chemistry.chemical_compound Crystallography chemistry Bombyx mori Heat shock protein Adenosine triphosphate Ambient pressure
Zdroj:	High Pressure Research. 33:258-264
ISSN:	1477-2299 0895-7959
DOI:	10.1080/08957959.2013.773324
Popis:	The small heat shock proteins (sHSPs) solubilize thermo-denatured proteins without adenosine triphosphate energy consumption to facilitate protein refolding. sHSP20.8 is one of the silkworm (Bombyx mori) sHSPs having only one cystein in the N-terminal domain: Cys43. We report a simple measurement of oligomeric transition of sHSP20.8 using high hydrostatic pressure native polyacrylamide gel electrophoresis (high hydrostatic pressure (HP) native polyacrylamide gel electrophoresis (PAGE)). At ambient pressure under oxydative condition, the native PAGE of thermal transition of sHSP20.8 oligomer displayed a cooperative association. In contrast, HP native PAGE clearly demonstrated that sHSP20.8 dissociated at 80 MPa and 25°C, and the resultant molecular species gradually reassociated with time under that condition. In addition, the reassociation process was suppressed in the presence of the reductant. These results are consistent with the idea that sHSP20.8 oligomer temporally dissociates at the first thermo-se...
Databáze:	OpenAIRE
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