Faculty of Science (ETDs)

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Browsing Faculty of Science (ETDs) by Department "Department of Biochemistry"

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    Control of serine dehydratase activity in rat liver
    (University of the Witwatersrand, Johannesburg, 2015-02-24) Abed, Suliman; Manchester, K.L.
    Gluconeogenesis from amino acids in the liver is enhanced when the utilisation of glucose is limited under various hormonal and dietary conditions, such as diabetes, starvation or administration of a carbohydrate free diet. Pyruvate is of great importance as a carbon source for gluconeogenesis, since the sequence of gluconeogenic reaction is initiated by carboxylation of pyruvate to oxaloacetate. From this point of view, an important physiological role is suggested for serine dehydratase, which catalyses the degradation of serine to pyruvate and ammonia. The relationship of serine dehydratase levels to gluconeogenic activities, however, is poorly understood, A study of the hormonal and dietary control of serine dehydratase activity was carried out in vivo and in vitro in rat liver. Serine dehydratase was assayed by the colorimetric method of Suda and Nakagawa (1971) and the enzymatic method of Wimhurst and Manchester (1973). Both these methods have been found to be suitable since they are in agreement with each other and also give results which compare favourably with other published values. Activities of serine dehydratase from fresh liver and in slices of liver cultured for various periods have been compared. Also a study of the activity of another soluble enzyme, lactic dehydrogenase, was undertaken and the in vivo and in vitro levels were compared.