Renature of Recombinant of Two Recombinant Fish Growth Hormones: Plecoglossus altivelis and Epinephelus awoara

 

Ya-Chi Sua* (蘇雅琪), Chia-Ching Changb (張家靖) and Lou-Sing Kana,c (甘魯生)

 

a. Institute of Biochemistry, Natinal Chung Hsing University, Taichung.

b. Deptartment Physics, National Dong Hwa University, Hualien.

c. Institute Chemistry, Academia Sinica, Nankang.

 

 

In this study we have renatured both structure and bio-function of two recombinant fish growth hormones (Plecoglossus altivelis and Epinephelus awoara), which are highly expressed in E. coli, from denature and aggregation forms. In order to monitor their conformational change gradually, stepwise restrain buffers are used and their conformation of folding intermediates can be detected by circular dichroism (CD) spectra. Dynamic light scattering analysis indicates gyration radius of each folding intermediate is uniform. This result suggests that renature processes are not a simple two state transition. Both gyration radius and CD profiles suggest that the conformation of those intermediates may in molten globule states. These stepwise refolding processes can create stable folding intermediates and this may help us to reveal possible protein folding mechanism.