Download Biochemistry of Zinc by Ananda S. Prasad PDF

By Ananda S. Prasad

In reaction to the global illnesses attributable to dietary zinc deficiency, coupled with the amazing advances in our wisdom of zinc metabolism, the writer has written this monograph at the scientific results of this crucial mineral. Dr. Prasad specializes in biochemical facets, but additionally contains chapters on toxicity and review ideas with a purpose to offer clinicians who come upon zinc similar difficulties of their perform with a realistic reference source.

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Extra info for Biochemistry of Zinc

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Thymus showed a greater decrease, whereas adrenal, pituitary, and kidney were heavier in zinc-deficient pigs. Serum zinc and alkaline phosphatase activity were decreased significantly in the zinc-deficient pigs. Zinc content of the bone, pancreas, and liver and activities of various zinc-dependent enzymes in bone, pancreas, testis, skin, esophagus, and pituitary were decreased in zinc-deficient pigs compared with the restrictedly fed controls. SOH showed no differences in its activities between the two groups.

Liver OCT activity in deficient rats gradually decreases, while in control rats it significantly increases with time. , and Prasad, A. , 1978. Plasma ammonia and liver ornithine transcarbamoylase activity in zinc deficient rats, Am. J. Physiol. 001 26 2-7). Activities of AST in liver and Glns in liver, muscle, and brain showed no significant alterations in zinc-deficient animals. The urea cycle is a major biochemical pathway where ammonia is produced and subsequently removed from the body by the synthesis of urea, and thus the assay of the activities of the urea cycle-related enzymes may provide an insight into the mechanism for hyperammonemia in zinc deficiency.

In mammalian cells DHO activity resides in a 240-kDa protein that also has carbamoylphospate synthetase and aspartate transcarbamylase activities. Only the DHO domain contains zinc that is essential for catalytic activity. This 44kDa domain contains seven thiols and one stable zinc. It is possible that some zinc ions may have been lost during isolation inasmuch as the zinc content of bacterial DHO varies with isolation procedure. According to this model (as shown in Fig. 2-5), dimeric zinc-dependent enzyme (DHO) with three zinc atoms per unit (on the left) on reaction with substrate or a chelator yields an active enzyme whose monomers contain only one zinc at the active site.

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