Journal of Nutrition

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Journal of Nutrition Vol. 111 No. 12 December 1981, pp. 2087-2097
Copyright © 1981 by American Society for Nutrition
This Article
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Preusch, P. C.
Right arrow Articles by Suttie, J. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Preusch, P. C.
Right arrow Articles by Suttie, J. W.

Vitamin K-Dependent Reactions in Rat Liver: Role of Flavoproteins1

Peter C. Preusch2 and John W. Suttie3

Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison, WI 53706

The role of flavins in vitamin K function was assessed by examining blood coagulation and in vitro activities of hepatic vitamin K-dependent enzymes from control and riboflavin-deficient rats. One-stage prothrombin times and Factor VII activities were lower in flavin-deficient rats than in ad libitum or pair-fed controls. Fibrinogen, prothrombin, and Factor X activities were normal. Hepatic vitamin K-dependent carboxylase activity was severely depressed in flavin-deficient rats when assayed with [vitamin K + NADH] and somewhat depressed with reduced vitamin K (vitamin KH2) as substrate. One-hour flavin repletion appreciably restored [vitamin K + NADH]-dependent activity, but vitamin KH2-dependent activity was not restored even after 16 hours repletion. These results suggest that the carboxylating enzyme itself is not a flavoprotein, but that the microsomal NADH dehydrogenase required for [vitamin K + NADH]-dependent carboxylation is a flavoprotein. This dehydrogenase may differ from the cytosolic Warfarin-inhibitable ‘DT-diaphorase’ in that the activity of the latter, which is reduced 50% in flavin-deficient rats, is not at all restored by one-hour flavin repletion. Flavin status-dependent differences in NADH-dependent or vitamin KH2-dependent epoxidation of vitamin K paralleled differences in the carboxylase. Flavin deficiency had no effect on vitamin K 2,3-epoxide reductase activity nor on its inhibition by Warfarin.


KEY WORDS: • dehydrogenases • flavoproteins • riboflavin • vitamin K

1 Supported in part by a grant from the National Institutes of Health (AM-14881).

2 National Institutes of Health Postdoctoral Fellow (HL-06136) and National Institutes of Health Postdoctoral Trainee (DE-07031).

3 To whom correspondence should be addressed.

Manuscript received 12 March 1981.





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]