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Abstract
We have developed a rapid, reliable procedure for the purification of rat hepatic glucokinase. The purification utilizes DEAE-cellulose, two affinity chromatography steps, and high-performance liquid chromatography. Glucokinase with a specific activity of 240 units/mg, a 42K-fold purification, and a yield of 60% is obtained. The enzyme appears as a homogenous band, with over 99% purity as assessed by polyacrylamide gel electrophoresis. The purification procedure can be completed in 5 days.