Purification and Characterization of s-CrystallinJQuinone Oxidoreductase from Camel Liver

Abstract

t;..Qystallln is a major protein In the lens of certain mammals. It has been characterized as a novel NADPH:quinone oxidoreductase, showing Hmlted quinone substrate specificity. Here we report fa- 1he first time, purification of this protein from camel liver by a sequential procedure of batch adsorption chromatography using CM-Sephadex C-50, affinity chromatography on Blue Sepharose CL-6B and 2', 5' ADP-Sepharose 4B columns. The pure material was isolated in a yield of 2.5% and purification fold of 253 over homogenate, with specific activity of 22 unitslmg protein. Kinetic and physical properties of this protein have been found to be similar with those of camel lens c,-aystallin.