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.
