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Division of Animal and Veterinary Science, College of Agriculture and Forestry, West Virginia University, Morgantown, West Virginia 26506
Taurine, a compound present in the tissues of all animals, is known to arise from cystine as well as through the utilization of sulfate-sulfur. Sulfate, activated by the action of ATP-sulfurylase (EC 2.7.7.4) to form adenosinephosphosulfate (APS) and APS-kinase (EC 2.7.1.25) to form 3'-phosphoadenosine-5'-phosphosulfate (PAPS), is then transferred to a carbon acceptor by the action of a sulfotransferase (EC 2.8.2). This enzymatic pathway in vitamin-deficient and control chicks was investigated to ascertain the role that vitamin-coenzymes may play in these reactions. Chicks were fed diets deficient in thiamin, riboflavin, vitamin B6, folic acid, vitamin A or vitamin D2 and the sulfate activation and sulfotransferase activities of these birds were assayed. Folic acid- and vitamin A-deficient chicks had lower ATP-sulfurylase and APS-kinase activity than the control birds. Pyridoxine was associated with sulfotransferase activity as evidenced by decreased in vitro taurine formation from PAPS. Vitamin D3-deficient chicks showed a lower rate of taurine synthesis in the liver when administered 35SO4 orally, whereas no difference was observed in taurine synthesis or PAPS formation in vitro.
KEY WORDS: taurine sulfate vitamin deflciencies
1 Published with the approval of the Director of the West Virginia Agricultural Experiment Station as Scientific Paper no. 1131.
Manuscript received 24 May 1971.