Drosophila lactate dehydrogenase: partial purification and characterization |
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| Authors: | M C Rechsteiner |
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| Affiliation: | 1. Department of Chemistry, Howard University, Washington DC 20059, United States;2. Department of Biology, Howard University, Washington DC 20059, United States;3. Department of Polymer Engineering, University of Akron, Akron, OH 44325, United States;4. Department of Microbiology, College of Medicine, Howard University, Washington DC 20059, United States;1. Department of Biological and Chemical Engineering, Bozhou Teachers College, 2266 Tangwang Road, Bozhou Anhui 236800, PR China;2. Institute of Materia Medica, Shandong Academy of Medical Sciences, Jinan 250062, PR China;3. School of Medicine and Life Science, University of Jinan, Shanghai 250200, PR China;1. School of Civil, Environmental and Architectural Engineering, Korea University, Seoul, 136-713 Republic of Korea;2. High-Temperature Energy Materials Research Center, Korea Institute of Science and Technology, Seoul, 136-791 Republic of Korea;1. Departamento de Química, Unidad Departamental de Química Analítica, Facultad de Ciencias, Universidad de La Laguna (ULL), San Cristóbal de La Laguna (Tenerife), España;2. Department of Chemistry, Centre for Analysis and Synthesis, Lund University, Lund, Sweden |
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| Abstract: | ![]()
Drosphila LDH has been purified 130-fold. It is similar to vertebrate skeletal muscle LDH in molecular weight and kinetics with pyruvate. Although Drosophila LDH exhibits only one band of activity in several electrophoretic systems, heat denaturation experiments indicate two forms of the enzyme. Neither form exhibits pyruvate kinetics similar to those of vertebrate heart LDH. |
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