Abstract
Lens Polyol dehydrogenase was purified approximately 1000-fold from calf lenses and the properties of the enzyme were studied. The enzyme appears to be a metallo-enzyme and is reactivated, after inhibition by EDTA, by magnesium ion. β-mETOH lowers the threshold concentration for magnesium ion. Furthermore, NADH prevents EDTA inhibition. The pH optima for the forward and reverse reactions were pH 9 and pH 7 respectively. The following K m values were determined: xylitol, 2·08 × 10 −3 m; sorbitol, 1 × 10 −2 m; NAD, 2·7 × 10 −5 m; and, fructose, 3·2 × 10 −2 m. Additionally, it was found that NADH, a product of the forward reaction, is an enzyme inhibitor. Thus, the concentration of sorbitol in the lens and the ratio of NAD NADH may play important roles in regulating the activity ofolyol dehydrogenase activity in vivo as well as in vitro.
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.
