Abstract
1. 1. In aortic wall, a xylosyl-transferase catalyses transfer of xylose, from UDP-xylose, to an endogenous acceptor. This enzyme is soluble (145,000 g supernatant). 2. 2. Its optimum pH is 6.7 and its optimum temperature is 37°C. Xylosyl-transferase has a good stability at supra-optimum temperature. 3. 3. Manganese is activator at millimolar concentration, whereas potassium and magnesium have no effect. 4. 4. The affinity constant for UDP-xylose substrate is equal to 3.5 μM/L. 5. 5. Inhibition of the enzyme system is obtained, in a rather notable way, by the nucleosides-di- and tri-phosphates with pyrimidic bases (UDP, CDP, UTP, CTP). 6. 6. The study of its behaviour in terms of the UDP-xylose concentration has led to the discovery of an activation by the substrate UDP-xylose. Very good purification is obtained by electrofocusing on ampholine column.
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