Abstract
The nucleotide dependence, tissue distribution and subcellular localization of glutamate dehydrogenase (GDH) (both reductive amination and oxidative deamination) were studied in a freshwater air-breathing teleost, Heteropneustes fossilis. The oxidative deamination reaction of GDH was absolutely dependent on ADP and the reductive amination reaction was independent of ADP. ADP acted as a positive modulator for the latter reaction. Both NADH and NADPH served equally well as coenzymes for reductive amination reaction whereas in the oxidative deamination reaction only NAD+ and not NADP+ acted as the coenzyme. GDH activity was found to be more stable in phosphate buffer than in Tris buffer. The enzyme activities were found to be at a maximum in liver followed by kidney, gill, muscle and brain. GDH activity was found to be mitochondrial in all the tissues studied. A three to four times higher reductive amination reaction than oxidative deamination reaction suggested an important role of GDH in ammonia detoxification in various tissues of H. fossilis.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
