By Ananda S. Prasad
In reaction to the global illnesses brought on by dietary zinc deficiency, coupled with the striking advances in our wisdom of zinc metabolism, the writer has written this monograph at the scientific results of this crucial mineral. Dr. Prasad makes a speciality of biochemical elements, but in addition comprises chapters on toxicity and overview suggestions with the intention to offer clinicians who come upon zinc comparable difficulties of their perform with a realistic reference source.
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Additional info for Biochemistry of Zinc
The activity of this enzyme is decreased in lead toxicity. Zinc supplementation both in vivo and in vitro reverses the inhibitory effect oflead on this enzyme. The human red cell o-ALD consists of eight subunits of 31 to 35 kDa. Each subunit contains one Zn2 + and treatment with oxygen or 5,5-dithiobis-(2nitrobenzoic acid) (DTNB) causes loss of zinc in parallel with inactivation of enzymatic function. , 1980). , 1980). Two cysteine and two histidine groups constitute the active site where the zinc resides.
We also studied the effects of zinc deficiency in young pigs (Prasad et a/.. 1969). Growth retardation was evident by the end of the first week and moderately severe parakeratosis was observed by the end of the second week. The weight of most organs decreased in proportion to the body weight. 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.
Each subunit of this enzyme contains two zinc atoms and binds one molecule of NAD(H). One zinc atom is essential for the catalytic activity and the function of the other zinc atom is unknown (noncatalytic). Inasmuch as complete removal of zinc does not affect the integrity of alcohol dehydrogenase Zinc and Enzymes ? ' 23 CYS-100 CYS-97 Figure 2-3. Schematic representation of the ligands and coordination geometry of the catalytic (left) and noncatalytic (right) zinc atoms of equine liver alcohol dehydrogenase.