Purification, Characterization and cDNA Cloning of the 200 kDa Protein Induced by Cold Acclimation in Wheat

摘要: We have purified to homogeneity the 200 kDa protein induced specifically by low temperature in wheat (Triticum aestivum L.). The boiling solubility of has been used as a main step purification procedure. Amino acid composition indicates that compositional bias for glycine (11.4%), threonine (13.3%), and alanine (22.0%). Using oligonucleotide probes, we isolated clone (p Wcs200) from cold-acclimated winter cDNA library. Northern analysis demonstrated expression corresponding gene was upregulated temperature. Southern showed organization relative copy number were identical two cultivars differing their capacity develop freezing tolerance. Protein sequence immunological analyses indicate this shares similar features with 50 during cold acclimation wheat. proteins are boiling-soluble, possess repeated elements. These elements may be important development shown is largest member family immunologically-related cold-induced Expression pWcs200 E. coli yielded product around kDa, indicating contains most coding region protein.