Abstract |
The sulfation of ascorbic acid by an ascorbic acid sulphotransferase was investigated using rat liver and colon homogenates. When Na2 35 SO4 or 3'-phosphoadenylyl [35S] sulfate (P-Ado-P-35S) and ascorbic acid were used as substrates, chromatographic behavior of the reaction products on thin-layer cellulose suggested that ascorbic acid 2-[35S] sulfate was formed. With Na2 35SO4 as the source of radioactive sulfate in the assay system, ATP was found to be an obligatory cofactor. Incorporation of [35S] sulfate frofrom Na2 35SO4 into ascorbic acid 2-[35S] sulfate was also decreased when ATP sulfurylase inhibitors were added to the system. P-Ado-O35S alone in the assay without ATP was an extemely effective sulfating agent. In addition, liver and colon homogenates from vitamin A deficient and sufficient rats were used in one of the studies. Vitamin A deficiency appeared to have little effect on ascorbic acid 2-sulfate formation.
|
Authors | M Mohamram, R B Rucker, R E Hodges |
Journal | Biochimica et biophysica acta
(Biochim Biophys Acta)
Vol. 437
Issue 1
Pg. 305-10
(Jun 23 1976)
ISSN: 0006-3002 [Print] Netherlands |
PMID | 949509
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
|
Chemical References |
- Sulfuric Acids
- Sulfurtransferases
- Ascorbic Acid
|
Topics |
- Animals
- Ascorbic Acid
(metabolism)
- Colon
(metabolism)
- Kinetics
- Liver
(metabolism)
- Organ Specificity
- Rats
- Sulfuric Acids
(metabolism)
- Sulfurtransferases
(metabolism)
- Vitamin A Deficiency
(metabolism)
|