Related Experiment Videos
Purification of streptodornase from Streptococcus equisimilis and its DNA-induced conformational change
1Department of Food Science and Technology, College of Agriculture, Chungnam National University, Taejon, Korea.
Biochemical and Biophysical Research Communications
|January 3, 1997
Abstract:
Extracellular streptodornase was purified from fermentation media of Streptococcus equisimilis by stepwise carboxymethyl-Sepharose column chromatography. The active enzyme fraction was eluted with phosphate buffer containing 0.2 M NaCl. The purified enzyme showed a homogeneity on SDS-PAGE and had a subunit molecular weight of 35 kDa. Conformational change of streptodornase by binding to calf thymus DNA was examined by circular dichroism (CD). CD study clearly showed a DNA-induced conformational change in the secondary structure of streptodornase, resulting in a decrease of alpha-helical content of the enzyme.