Abstract
1.1. Neuraminidase (N-acetylneuraminate glycohydrolase, EC 3.2.1.18) from the chorioallantois of the 19-day-old chick embryo has been isolated and studied.2.2. The isolation procedure consisted of mild extraction of the washed membranes, heat treatment, precipitation with ammonium sulphate and chromatography on a column of hydroxyl apatite. The final product is about 200-fold purer than the starting fluid.3.3. The purified preparation is stable at o° but unstable at 37°. It has a sedimentation coefficient of about 3.3 S and is inactivated by sulfhydryl reactants. The pH of optimum activity on three substrates, sialyl lactose, fetuin and ovine submaxillary gland mucin is between 5 and 4. Values for Km and maximum rates of action on these substrates have been determined.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects
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