Open AccessThermally induced aggregation and its suppression of silkworm small heat shock protein sHSP19.9
Author(s) -
Muhammad Tofazzal Hossain,
Yoichi Aso
Publication year - 2017
Publication title -
animal science journal of pakistan
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