Studies on Neuraminidase Activity of the Rabbit Endometrium

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Abstract
The homogenate of endometrium, scraped from uterus of the superovulated rabbit, shows a pronounced neuraminidase activity which is different from the uterine factor. The enzyme has an optimum at pH 5.2 and is strongly inhibited by Zn2+, Hg2+, Fe2+ and Fe3+ ions. The apparent Km values with fetuin, N-acetylneuramin lactose and Cowper’s gland mucin are 0.36 x 10-5 M, 80 x 10-5 M and 0.54 x 10-5 M, respectively. Preincubation at 37°C results in decreased activity of the endometrial neuraminidase. The enzyme is inactivated by sonication, freezing and thawing. EDTA, glutathione and iodoacetate have no effect on the enzyme activity.