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Jinn TL, Chen YM, Lin CY. Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean. Plant Physiol. 1995;108(2):693-701doi: 10.1104/pp.108.2.693.
Jinn, T. L., Chen, Y. M., & Lin, C. Y. (1995). Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean. Plant physiology, 108(2), 693-701. https://doi.org/10.1104/pp.108.2.693
Jinn, T. L., et al. "Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean." Plant physiology vol. 108,2 (1995): 693-701. doi: https://doi.org/10.1104/pp.108.2.693
Jinn TL, Chen YM, Lin CY. Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean. Plant Physiol. 1995 Jun;108(2):693-701. doi: 10.1104/pp.108.2.693. PMID: 12228501; PMCID: PMC157390.
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Plant Physiol. 1995 Jun;108(2):693-701. doi: 10.1104/pp.108.2.693.

Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean.

Plant physiology

T. L. Jinn, Y. M. Chen, C. Y. Lin

Affiliations

  1. Department of Botany, National Taiwan University, Taipei, Taiwan.

PMID: 12228501 PMCID: PMC157390 DOI: 10.1104/pp.108.2.693

Abstract

Examination of an ammonium sulfate-enriched fraction (70-100% saturation) of heat-shock proteins (HSPs) by nondenaturing polyacrylamide gel electrophoresis revealed the presence of a high molecular mass complex (280 kD) in soybean (Glycine max) seedlings. This complex cross-reacted with antibodies raised against soybean class I low-molecular-mass (LMW) HSPs. Dissociation of the complex by denaturing polyacrylamide gel electrophoresis showed the complex to contain at least 15 polypeptides of the 15-to 18-kD class I LMW HSPs that could be detected by staining, radiolabeling, and western blotting. A similar LMW-HSP complex was observed in mung bean (Vigna radiata L.; 295 kD), in pea (Pisum sativum L.; 270 kD), and in rice (Oryza sativa L.; 310 kD). The complex was stable under high salt conditions (250 mM KCI), and the integrity was not affected by 1% Nonidet P-40 and 3 [mu]g/ML RNase treatment. The size of the isolated HSP complex in vitro was conserved to 55[deg]C; however, starting at 37.5[deg]C, it changed to higher molecular forms in the presence of soluble proteins. The isolated HSP complex was able to protect up to 75% of the soluble proteins from heat denaturation in vitro.

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