Abstract
The first thermophilic eubacterial glutamate dehydrogenase was purified to homogeneity from Bacillus acidocaldarius to compare its molecular properties with those of the glutamate dehydrogenase from thermophilic archaea. Glutamate dehydrogenase represents 2% of the total soluble proteins of B. acidocaldarius, an amount that may suggest an important role for this enzyme in nitrogen metabolism of the thermophilic eubacterium. The protein is a hexamer (subunit mass 48 kDa) and undergoes dissociation during gel filtration analysis. Isoelectric focusing of the purified enzyme indicated a pI of 4.5. The enzyme is strictly specific for NAD, 2-oxoglutarate, and l-glutamate. The thermal stability of B. acidocaldarius glutamate dehydrogenase is dependent on protein concentration.
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 callMore From: Comparative Biochemistry and Physiology -- Part B: Biochemistry and Molecular Biology
Disclaimer: 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.
