Abstract
1. 1. A C-type lactate dehydrogenase isozyme has been purified to homogeneity from the liver of the Atlantic cod. 2. 2. The enzyme consists of four identical subunits each with a mol. wt of 35,000. 3. 3. Optimum concentrations, K ms, and relative activities were determined for various substrates along with the optimum pH for the reaction with pyruvate and lactate. 4. 4. Glyoxalate, α-ketobutyrate, α-ketovalerate, and α-ketoglutarate were significantly reduced but branched chain α-ketoacids were not utilised as substrates. 5. 5. Substrate inhibition was observed for both lactate and pyruvate as is generally found for B-type lactate dehydrogenase isozymes but the lactate optimum concentration and K m more closely resemble the A-type lactate dehydrogenases.
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.
