Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

6 children with idiopathic nephrotic syndrome were investigated during clinical relapse to examine the interrelation between distal urinary acidification and urinary sodium excretion. Blood and urine studies were initiated 4 h after completion of ammonium chloride loading, prior to and following the intravenous administration of furosemide. Values for plasma bicarbonate before and after furosemide administration were not significantly different. In the control periods, when urinary sodium excretion was very low, a defect in urinary acidification was demonstrated (UPH: 6.09 +/- (SD) 0.27; UTAV and UNH4V: 12.6 +/- 3.1 and 36.4 +/- 15.8 mumol/min/1.73 m2, respectively.) Following furosemide-induced natriuresis UPH fell to 4.81 +/- 0.25 (p less than 0.0005), and UTA2V and UNH4V increased to 46.3 +/- 15.8 and 125.6 +/- 49.5 mumol/min/1.73 m2, respectively (p less than 0.002). No overall correlation existed between urinary acidity, both considered as hydrogen ion concentration and as hydrogen ion excretion, and rate of urinary sodium excretion; but significant correlations were present between hydrogen ion concentration in the urine and both UC1V-UNAV (r = 0.38, p less than 0.05), and UC1V - (UNaV + UKV) (r = 0.64, p less than 0.01). These results indicate that the defect in distal urinary acidification observed in nephrotic syndrome is probably due to decreased delivery of sodium to the distal nephron. The enhanced secretion of hydrogen ion observed after furosemide administration may be related both to increased sodium delivery and to greater sodium than chloride reabsorption in the collecting duct.
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PMID:Defect in urinary acidification in nephrotic syndrome and its correction by furosemide. 716 8

The YUH1 gene coding for ubiquitin C-terminal hydrolase 1, a deubiquitinating enzyme, was cloned from the Saccharomyces cerevisiae genomic DNA and expressed in Escherichia coli. YUH1 was fused with the 6 histidine tag at the N-terminus (H6YUH1) or C-terminus (YUH1H6) and purified by an immobilized metal affinity chromatography with high purity. By using a fluorogenic substrate, Z-Arg-Leu-Arg-Gly-Gly-AMC, the deubiquitinating activities for H6YUH1 (1.72U/mg) and YUH1H6 (1.61U/mg) were about 18 times higher than 0.092U/mg for H6UBP1, ubiquitin specific protease 1 of S. cerevisiae containing the 6 histidine residue at the N-terminus which is normally used in protein engineering. YUH1 had the optimal temperature of 27 degrees C and acidity of pH 8.5. Analysis of thermal deactivation kinetics of H6YUH1 estimated 3.2 and 1.4h of half lives at 4 and 52 degrees C, respectively. Immobilization onto the Ni-NTA affinity resin and environmental modulation were carried out to improve the stability of YUH1. Incubation of the immobilized YUH1 in 50% glycerol solution at -20 degrees C resulted in 52% of decrease in specific activity for 7days, corresponding to a 2.7-fold increase compared with that of the free YUH1 incubated in the same solution at 4 degrees C.
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PMID:Characterization of ubiquitin C-terminal hydrolase 1 (YUH1) from Saccharomyces cerevisiae expressed in recombinant Escherichia coli. 1770 60