Abstract
sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggregation was suppressed in the presence of dithiothreitol and at high ionic strength. In contrast, sHSP20.8 was not aggregated. Aggregation of sHSP19.9 was partially suppressed by sHSP20.8 and in the presence of catalase as a target protein. Based on changes in small-angle X-ray scattering, it is possible that the molecular size of sHSP19.9 is larger than that of sHSP20.8, and that their molecular sizes increase with increasing temperature in a reversible, biphasic manner. sHSPs did not protect catalase from thermal inactivation, but protected it from precipitation by forming a soluble complex. sHSP20.8 and sHSP19.9 with dithiothreitol were stable against lyophilization, autoclaving at 120 °C, and boiling.
| Original language | English |
|---|---|
| Pages (from-to) | 1556-1563 |
| Number of pages | 8 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 74 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Sep 1 2010 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry
Cite this
Structural properties of silkworm small heat-shock proteins:SHSP19.9 and sHSP20.8. / Hossain, MD Tofazzal; Teshiba, Satoshi; Shigeoka, Yuichi; Fujisawa, Tetsuro; Inoko, Yoji; Sakano, Daisuke; Yamamoto, Kohji; Banno, Yutaka; Aso, Yoichi.
In: Bioscience, Biotechnology and Biochemistry, Vol. 74, No. 8, 01.09.2010, p. 1556-1563.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Structural properties of silkworm small heat-shock proteins:SHSP19.9 and sHSP20.8
AU - Hossain, MD Tofazzal
AU - Teshiba, Satoshi
AU - Shigeoka, Yuichi
AU - Fujisawa, Tetsuro
AU - Inoko, Yoji
AU - Sakano, Daisuke
AU - Yamamoto, Kohji
AU - Banno, Yutaka
AU - Aso, Yoichi
PY - 2010/9/1
Y1 - 2010/9/1
N2 - sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggregation was suppressed in the presence of dithiothreitol and at high ionic strength. In contrast, sHSP20.8 was not aggregated. Aggregation of sHSP19.9 was partially suppressed by sHSP20.8 and in the presence of catalase as a target protein. Based on changes in small-angle X-ray scattering, it is possible that the molecular size of sHSP19.9 is larger than that of sHSP20.8, and that their molecular sizes increase with increasing temperature in a reversible, biphasic manner. sHSPs did not protect catalase from thermal inactivation, but protected it from precipitation by forming a soluble complex. sHSP20.8 and sHSP19.9 with dithiothreitol were stable against lyophilization, autoclaving at 120 °C, and boiling.
AB - sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggregation was suppressed in the presence of dithiothreitol and at high ionic strength. In contrast, sHSP20.8 was not aggregated. Aggregation of sHSP19.9 was partially suppressed by sHSP20.8 and in the presence of catalase as a target protein. Based on changes in small-angle X-ray scattering, it is possible that the molecular size of sHSP19.9 is larger than that of sHSP20.8, and that their molecular sizes increase with increasing temperature in a reversible, biphasic manner. sHSPs did not protect catalase from thermal inactivation, but protected it from precipitation by forming a soluble complex. sHSP20.8 and sHSP19.9 with dithiothreitol were stable against lyophilization, autoclaving at 120 °C, and boiling.
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U2 - 10.1271/bbb.100131
DO - 10.1271/bbb.100131
M3 - Article
VL - 74
SP - 1556
EP - 1563
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 8
ER -