Abstract
Antibodies prepared against two major polypeptides of the 15- to 18-kD class of soybean heat shock proteins (HSPs) individually reacted with its antigen and cross-reacted with 12 other 15- to 18-Kd HSPs. We also found that this antibody preparation cross-reacted with the same class low molecular weight (LMW) HSPs of mung bean, rice and other seven plant species tested based on western blot analysis. The 70 to 100% ammonium sulfate (AS) fraction from heat shocked seedlings of mung bean and rice, as in soybean, contained a high percentage of all the HSPs. The proteins in this fraction were resistant to heat denaturation, as judged by their unpelletability after heat treatment. Moreover, this fraction showed a significant ability to protect the soluble proteins from heat denaturation. The HSPsenriched fractions prepared from mung bean and rice heat shocked seedlings were able to thermostabilize the homologous soluble proteins. Additionally, the HSPs-enriched fractions were exchangeable among these three plant species for thermostabilization.
In soybean, when the HSPs-enriched fraction depleted of the 15- to 18-kD class HSPs, the effectiveness in prevention of heat denaturation was lost. However, when the 15- to 18-kD HSPs recovered in the AS fraction, the thermostabilization was restored again. This suggests that the HSPs of 15- to 18-kD class are important for providing the protection from heat denaturation.
Supported by National Science Council of Taiwan under grants NSC 78-0211-B002-02, NSC 79-0211-B002-02 and NSC 80-0211-B002-02.
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Lin, CY., Jinn, TL., Hsieh, MH., Chen, YM. (1994). Class I low molecular weight heat shock proteins in plants: immunological study and thermoprotection against heat denaturation of soluble proteins. In: Cherry, J.H. (eds) Biochemical and Cellular Mechanisms of Stress Tolerance in Plants. NATO ASI Series, vol 86. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79133-8_7
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DOI: https://doi.org/10.1007/978-3-642-79133-8_7
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