Isolation and properties of lactate dehydrogenase isozyme X from Swiss mice |
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| Authors: | C Wong R Ya?ez D M Brown A Dickey M E Parks R W McKee |
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| Affiliation: | 1. Faculty of Economics and Center for Advanced Studies in Management and Economics (CEFAGE), University of Algarve, Portugal;2. University of Strathclyde, Department of Management Science, UK;3. Ex-employee of HM Revenue & Customs, UK;1. Department of Neurology, Icahn School of Medicine at Mount Sinai, NY, New York, USA 10029;2. Precision Immunology Institute and Department of Genomic Sciences, Icahn School of Medicine at Mount Sinai, NY, New York, USA 10029;3. Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA 10029;4. Icahn Institute of Genomics and Multiscale Biology, Icahn School of Medicine at Mount Sinai, New York, NY, USA 10029;5. Geriatric Research, Education and Clinical Center, James J. Peters Veterans Affairs Medical Center, Bronx, New York, USA 10468;6. New Use Agriculture and Natural Plant Products Program, Department of Plant Biology, Rutgers University, New Brunswick, NJ, USA 08901;7. Department of Medicinal Chemistry, Ernest Mario School of Pharmacy, Piscataway, NJ, USA 08854;8. Department of Neurology, Johns Hopkins School of Medicine, Baltimore, USA, MD 21205;9. Solomon H. Snyder Department of Neuroscience, Johns Hopkins School of Medicine, Baltimore, USA, MD 21205;10. Department of Internal Medicine, Division of Neurology, Showa University School of Medicine, Tokyo, Japan;11. Department of Pharmacology, Showa University School of Medicine, Tokyo, Japan |
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| Abstract: | Lactate dehydrogenase X, a sixth LDH isozyme in testes and mature sperm, has been purified to homogeneity from adult mouse testes. The isozyme has a molecular weight of 139,000 ± 6000. Dissociation of the molecule with 6 m guanidine produced a homogeneous material with mol wt 37,700 ± 800. Pyruvate at 37 ° was reduced optimally at about pH 7.25 and a concentration of 0.25 mm. Alpha-ketobutyrate has an optimum pH of 7.75 and concentration of 0.5 mm for reduction with a rate about 50% greater than that of pyruvate. Alpha-ketoglutarate has an optimum pH of about 5.5 and is reduced at only about one-fourth the rate of pyruvate. Pyruvate reduction is considerably inhibited by 2.5 mmlactate. Alpha-hydroxybutyrate and α-hydroxyvalerate are oxidized at about the same rate and under similar optimum conditions as lactate. Alpha-hydroxyglutarate is oxidized at only about one-twentieth the rate of lactate. |
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