Human brain hypoxanthine guanine phosphoribosyltransferase: structural and functional comparison with erythrocyte hypoxanthine guanine phosphoribosyltransferase |
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| Authors: | K Ikeda H Suzuki S Nakagawa |
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| Affiliation: | 1. Department of Surgery, Jacobs School of Medicine, University of Buffalo, Buffalo, NY 14215, USA;2. Department of Biotechnology, National Institute of Pharmaceutical Education and Research, Sector 67, S.A.S. Nagar, Punjab 160062, India;3. Department of Biotechnology, Delhi Technological University, Delhi 110042, India;4. School of Chemistry and the Analytical and Biological Chemistry Research Facility (ABCRF), University College Cork, College Road, T12 YN60 Cork, Ireland |
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| Abstract: | A rapid and simple method, based on GMP Sepharose affinity chromatography, was used for the purification of human brain hypoxanthine guanine phosphoribosyltransferase. 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. The Km values for hypoxanthine and phosphoribosyl pyrophosphate were 50 and 111 microM, respectively. The Ki values for GMP and IMP with phosphoribosyl pyrophosphate were 21 and 37 microM, respectively. The purified enzyme from human brain did not differ significantly from the human erythrocyte one in amino acid composition. The brain and erythrocyte hypoxanthine guanine phosphoribosyltransferases showed complete immunochemical identity on Ouchterlony double diffusion. |
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