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.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call