Thermally induced aggregation and its suppression of silkworm small heat shock protein sHSP19.9 | Zendy

Muhammad Tofazzal Hossain | Zendy; Yuji Aso | Zendy

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Thermally induced aggregation and its suppression of silkworm small heat shock protein sHSP19.9

Author(s) -

Muhammad Tofazzal Hossain,

Yuji Aso

Publication year - 2017

Publication title -

bangladesh journal of animal science

Language(s) - English

Resource type - Journals

eISSN - 2408-8307

pISSN - 0003-3588

DOI - 10.3329/bjas.v46i1.32179

Subject(s) - dithiothreitol , heat shock protein , ionic strength , chemistry , cysteine , biophysics , chaperone (clinical) , biochemistry , heat stability , biology , gene , enzyme , materials science , organic chemistry , pathology , aqueous solution , composite material , medicine

About ten genes responsible for small heat-shock proteins (sHSP) have been isolated from silkworm. sHSP19.9 is one of the important member among them. Heat-induced stability of the sHSP was investigated at 60ºC with 20 mM HEPES buffer pH 7.7 containing 10 mM NaCl (low-ionic strength). Along with it probable suppression of the aggregation was also examined. At the mentioned reaction medium, sHSP19.9 was observed to be aggregated on the concentration- and time-dependent manners. It was successfully suppressed with dithiothreitol (DTT), higher-ionic strengths, Cysteine residues modifications and molecular chaperone: sHSP20.8.Bang. J. Anim. Sci. 2017. 46 (1): 57-64

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