Control of serine dehydratase activity in rat liver
Date
2015-02-24
Authors
Abed, Suliman
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Abstract
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.
Description
Thesis (M.Sc.(Biochemistry))--University of the Witwatersrand, Faculty of Science, 1980.