Abstract
L-Gulono-γ-lactone oxidase catalyzes the last step in the biosynthesis of L-ascorbic acid in animals. This chapter discusses L-gulono-γ-lactone oxidase. Humans, primates, and guinea pigs are unable to synthesize this vitamin, because they lack this enzyme. The L-ascorbic acid formed can be determined colorimetrically by the 2,4-dinitrophenylhydrazine method or by the reduction of Fe 3+ to Fe 2+, followed by coupling of the Fe2+ with α,α′ -dipyridyl. These methods are used to assay crude tissue preparations provided that corrections are made for endogenous L-ascorbic acid. The dehydrogenase activity of the enzyme can be measured spectrophotometrically by the reduction of 2,6-dichlorophenolindophenol in the presence of phenazine methosulfate. The purification of the enzyme from goat liver is described in the chapter.
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.
