AJCN Cancer Health Disparities Conference
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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 Adelekan, D. A.
Right arrow Articles by Thurnham, D. I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Adelekan, D. A.
Right arrow Articles by Thurnham, D. I.
Agricola
Right arrow Articles by Adelekan, D. A.
Right arrow Articles by Thurnham, D. I.

American Journal of Clinical Nutrition, Vol 46, 86-90, Copyright © 1987 by The American Society for Clinical Nutrition, Inc

ORIGINAL RESEARCH COMMUNICATIONS

Dependence of pyridoxine metabolism on riboflavin status in sickle cell patients

DA Adelekan, AD Adekile and DI Thurnham

The relationship between riboflavin and pyridoxine status was studied in 40 patients with sickle cell disease (SCD) and 12 normal children by measuring activation coefficients of erythrocyte glutathione reductase (EGRAC) and aspartate transaminase (ASTAC). Prevalence of riboflavin deficiency was significantly lower in SCD (42.5%) than in control subjects (83%) and there was less pyridoxine deficiency in SCD (10.3%) than control subjects (54.5%). Aspartate transaminase (AST) activities in SCD patients were double those in control subjects. Pyridoxine status of patients, but not of control subjects, was directly affected by riboflavin status as judged from significant correlations between EGRAC and both AST activity and ASTAC. Poor riboflavin status in patients may be restricting availability of pyridoxal phosphate (PLP) due to combined effects of enhanced PLP requirements and effects of poor riboflavin status on the synthesis of PLP by pyridoxine phosphate oxidase (PPO). PPO activity was no different in the two groups.




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1987 by The American Society for Nutrition