Purification and Characterization of ζ-Crystallin/Quinone Oxidoreductase
from Camel Liver
Abstract:
ζ-Crystallin is a major protein in the lens of certain mammals. It has been characterized as a novel NADPH: quinone oxidoreductase, showing limited quinone substrate specificity. This study report for the first time purification of this protein from camel liver by a sequential procedure of batch adsorption chromatography using CM-Sephadex C-50, affinity chromatography using Blue Sepharose CL-6B and 2`, 5` ADP-Sepharose 4B. The pure material was isolated in a yield of 2.5% and purification fold of 253 over homogenate, with specific activity of 22 units/mg protein. Kinetic and physical properties of this protein have been found to be identical with those of camel lens ζ-crystallin.
How to cite this article
Abdulaziz A. AI-Hamidi , 2004. Purification and Characterization of ζ-Crystallin/Quinone Oxidoreductase
from Camel Liver. Pakistan Journal of Biological Sciences, 7: 1772-1776.
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