Both α crystallin from bovine eye lens and Hsp16.3 from Mycobacterium tuberculosis are members of the small heat shock protein family. They were preincubated at 100 ℃ for 15 min and then cooled on ice immedi...Both α crystallin from bovine eye lens and Hsp16.3 from Mycobacterium tuberculosis are members of the small heat shock protein family. They were preincubated at 100 ℃ for 15 min and then cooled on ice immediately. The chaperone like activities of preheated proteins were measured at 37 ℃ using DTT treated insulin B chains as substrates. Both preheated proteins exhibited greatly enhanced chaperone like activities, accompanied with almost unchanged secondary structures and surface hydrophobicity but with a minor change in tertiary structures. The dramatically enhanced chaperone like activities of preheated α crystallin and Hsp16.3 may have resulted from the irreversible change in the tertiary structure as detected by near UV CD spectra. 展开更多
基金Supported by the National Natural Science Foundation of China ( No.3 970 0 0 2 5 ) and the National Science Foundation for Outstanding Young Scientists in China ( No.3 972 5 0 0 8)
文摘Both α crystallin from bovine eye lens and Hsp16.3 from Mycobacterium tuberculosis are members of the small heat shock protein family. They were preincubated at 100 ℃ for 15 min and then cooled on ice immediately. The chaperone like activities of preheated proteins were measured at 37 ℃ using DTT treated insulin B chains as substrates. Both preheated proteins exhibited greatly enhanced chaperone like activities, accompanied with almost unchanged secondary structures and surface hydrophobicity but with a minor change in tertiary structures. The dramatically enhanced chaperone like activities of preheated α crystallin and Hsp16.3 may have resulted from the irreversible change in the tertiary structure as detected by near UV CD spectra.
