Abstract
1. 1. A rapid and simple method, based on GMP Sepharose affinity chromatography, was used for the purification of human brain hypoxanthine guanine phosphoribosyltransferase. 2. 2. A single protein band was detected by polyacrylamide gel electrophoresis of the native purified enzyme. A subunit molecular weight of 25,000 was estimated by SDS gel electrophoresis. 3. 3. The K m values for hypoxanthine and phosphoribosyl pyrophosphate were 50 and 111μM, respectively. The K i values for GMP and IMP with phosphoribosyl pyrophosphate were 21 and 37 μM, respectively. 4. 4. The purified enzyme from human brain did not differ significantly from the human erythrocyte one in amino acid composition. 5. 5. The brain and erythrocyte hypoxanthine guanine phosphoribosyltransferases showed complete immunochemical identity on Ouchterlony double diffusion.
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