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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a series of four experiments, asparaginase and glutaminase activity was measured in liver and kidney tissue of 7- to 19-day-old male broiler chicks. In Experiment 1, chicks were fed purified amino acid diets with 14.8 and 44.6% protein equivalents (PE) with 1, 3, or 5% added sodium bicarbonate. In Experiments 2, 3, and 4 the chicks were fed a 23% protein basal control diet, basal diet containing 5% ammonium chloride, and basal diet containing 5% ammonium chloride with 5 or 10% sodium bicarbonate, asparagine, or glutamine. In Experiments 2 and 4 the chicks were also fed 25, 50, or 75% protein-isolated soy-purified diets. The 44.6% PE diet increased liver and kidney asparaginase activity in chicks as compared to chicks fed a 14.8% PE diet. The addition of sodium bicarbonate to the 44.6% PE amino acid diet decreased the kidney asparaginase activity equivalent to kidney asparaginase activity of chicks fed the 14.8% PE diet. Asparaginase activity increased 4-fold in the kidneys of chicks fed the 23% protein basal diet containing 5% ammonium chloride and the pH of the urine from the chicks was 4.9. Chicks fed basal diets with 5% ammonium chloride plus 10% sodium bicarbonate or asparagine had the same kidney asparaginase activity and urine pH as chicks fed the 23% protein basal control diet. Glutamine added to chick diets containing 5% ammonium chloride did not decrease the kidney asparaginase activity or the urine acidity. Liver asparaginase activity was not increased in acidotic chicks fed diets with 5% ammonium chloride. The asparaginase activity of liver and kidney tissue were both significantly increased in chicks fed 75% protein-isolated soy purified diets and the pH of their urine was 5.6. The increase in liver asparaginase of chicks fed 75% protein or 44.5% PE diets was probably due to an endocrine gluconeogenic response producing increased catabolism of the majority of amino acids. The increase in kidney asparaginase of chicks fed 75% protein, 44.5% PE diets, and 23% protein basal diets with 5% ammonium chloride was primarily related to metabolic acidosis. Phosphate-dependent glutaminase (PDG) activity was localized in chick kidney mitochondria and was heat sensitive (55 C for 30 sec). The phosphate-independent glutaminase (PIG) activity was primarily localized in chick kidney mitochondria but was stable to a temperature of 55 C for 30 sec.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Asparagine and glutamine metabolism in chicks. 632 68

L-Asparaginase from Escherichia coli was coupled with two types of comb-shaped copolymer of poly-(ethylene glycol) derivative and maleic anhydride (activated PM), having molecular weights of 13,000 and 100,000 (activated PM13 and PM100, respectively) with multivalent reaction sites. After single intravenous injections of PM100-asparaginase and nonmodified asparaginase into rats, the enzymic activity of PM100-asparaginase in serum was well retained for at least 11 days, and the serum L-asparagine concentration remained undetectable for 27 days. The half-lives of PM100-asparaginase and nonmodified asparaginase were 50 and 1.5 h, respectively. Stabilization of L-asparaginase toward heat, urea, and acidity was caused by modifying the enzyme with activated PM13 and PM100. Especially, PM100-asparaginase retained high enzymic activity toward heat and urea, compared with PM13-asparaginase. It was suggested that these modifiers with a comb-shaped form and with multivalent reactive sites cover the whole surface of the asparaginase molecule and stabilize its conformation possibly through multiple covalent bindings and through various noncovalent interactions.
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PMID:Stabilization of L-asparaginase modified with comb-shaped poly(ethylene glycol) derivatives, in vivo and in vitro. 794 93