Abstract
A diaphorase was isolated from Lactobacillus casei and purified approximately ninetyfold. It has been shown to be free from DPNH oxidase and DPNH peroxidase activity. The enzyme is specific for DPNH rather than TPNH and requires the addition of FMN for maximal activity. A number of dyes will serve as acceptors, including p benzoquinone, indophenol, and ferricyanide. Oxygen, hydrogen peroxide, methylene blue, lipoic acid, cytochrome c, and substrate amounts of flavin nucleotides are inactive as acceptors. Under the assay conditions used, the diaphorase activity was only slightly inhibited by the presence of hydrogen peroxide, cyanide, or N-ethylmaleimide and not inhibited at all by versene or amytal.
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.
