Abstract
1. 1. Aortic xylosyl-transferase has been purified by isoelectric focusing. 2. 2. It appears as a single molecular species. 3. 3. It catalyses xylose transfer on an exogenous polypeptide acceptor. poly- l-serine. 4. 4. Optimal activity of the enzyme is pH 7.2. and a temperature of 57°C. 5. 5. The phenomenological study of this enzyme involving 2 substrates and 2 products are in agreement with ordered Bi-Bi mechanism. 6. 6. Possible relations with Theorell-Chance mechanism are discussed.
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