Oral zinc therapy in Indian childhood cirrhosis.
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Biomedical subjects
Publications and source records attributed to B Bhandari.
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Twenty-seven histopathologically proved cases of Indian childhood cirrhosis (ICC), 13 parents (father and mother) and nine siblings of ICC patients were studied from serum and urinary Cu, Zn, Mg and Cd levels by Atomic Absorption Spectrophotometer (AAS). Milk and drinking water from various sources were analysed for Cu, Zn, Mg and Cd contents, as was milk boiled and stored for up to six hours in various utensils. Serum and urinary Cu excretion were high (P less than 0.001) in ICC patients and within normal limits in siblings and parents. In ICC patients most hepatocytes contained multiple, coarse and dark brown orcein staining granules representing Cu associated protein. Serum Zn was low and urinary Zn excretion high in ICC patients (P less than 0.001 and P less than 0.01 respectively) and within normal limits in siblings and parents. Mg and Cd in serum and urine of ICC patients, siblings and parents were within normal limits. Cu content of milk boiled and stored in peetal (brass) utensils was high and directly related to the duration of storage; there was no change in Cu level in milk boiled and stored in steel and aluminium utensils. Zn, Mg and Cd levels in milk boiled and stored in peetal (brass) utensils remained unchanged. The levels of these elements in drinking water from various sources were also within limits as recommended by WHO (1971). Milk boiled and stored in peetal (brass) utensils seemed to account for increased Cu intake. Excessive Cu intake in ICC should be eliminated by avoiding brass utensils for boiling and storing milk. Some treatment to chelate excess Cu is also warranted.
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Nitrosomonas europaea oxidizes ammonia to nitrite, thereby deriving energy for growth. Glutamate dehydrogenase (NADP+) (EC 1.4.1.4) is the main route for the incorporation of ammonia into glutamic acid, because glutamate synthase (NADPH)(EC 1.4.1.13) was not detected in cell-free extracts of N. europaea. Some properties of a partially purified glutamine synthetase (EC 6.3.1.2) have been determined, namely the effects of pH and metal ions, substrate requirements, Km and Ki values, based on biosynthetic and gamma-glutamyltransferase (EC 2.3.2.2) assays. The molecular weight of the enzyme preparation was approximately 440 000. The gamma-glutamyltransferase activity was markedly inhibited by alanine, lysine, glutamic acid, aspartic acid and serine and to a lesser extent by glycine, asparagine, arginine and histidine. Except for tryptophan and cystine, the gamma-glutamyltransferase activity was inhibited to a greater extent by these amino acids than was the biosynthetic activity. Different pairs of amino acids in various combinations resulted in a cumulative inhibition of enzyme activity determined by either method. Of the various nucleotides tested, the gamma-glutamlytransferase activity of the enzyme was inhibited to a greater extent by di- and triphosphate nucleotides--IDP, CDP, UDP, ITP, CTP, TTP and ATP (except GDP and GTP) than by monophosphate nucleotides except AMP. Saturating concentrations of pyruvate, oxalate, oxaloacetate and alpha-ketoglutarate depressed enzyme activity. Various combinations of amino acids with adenine nucleotides exerted cumulative inhibitory effects on the transferase activity.
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