Class I low molecular weight heat shock proteins in soybean:purification, characterization, physiological biochemical function analysis and immunolocalization

• Main Authors: Jin, Zong Luo, 靳宗洛
• Other Authors: Lin, Qiu Rong
• Format: Others
• Language: zh-TW
• Published: 1995
• Online Access: http://ndltd.ncl.edu.tw/handle/55153889313229920168

博士 === 國立臺灣大學 === 植物學研究所 === 83 === 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 (280kD) 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.; 270kD), and in rice (Oryza sativa L.; 310 kD). The complex was stable under high salt conditions (250 mM KCl), 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.degree.C; however, starting at 37.5.degree.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.