Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum inorganic pyrophosphate (PPi) levels were consistently two- to threefold higher than plasma PPi prepared from the same blood. PPi was found in platelets in amounts ranging from 1.4 to 3 nmol/10(8) cells, using three different techniques for quantification. These levels are approximately 800 times higher than the mean PPi concentration in normal plasma and approximate the levels of ADP found in platelets by other workers. About 50% of platelet PPi was specifically released extracellularly after stimulation with thrombin. Timed release experiments showed a pattern of release that resembled that described for ADP and ATP. This pattern was clearly different from that shown by platelet calcium, serotonin, or beta-glucuronidase. Platelet inorganic pyrophosphatase was not released into the supernate in detectable amounts. Platelets from patients with nucleotide storage pool deficiency showed greatly reduced levels of PPi as compared with control. There was no detectable release of PPi into extracellular medium after thrombin addition to a suspension of these platelets.
 ...
PMID:Identification of inorganic pyrophosphate in human platelets and its release on stimulation with thrombin. 435 60

1. Chicken brain arylsulphatase A was purified 2000-fold, with overall recovery 14%, by using ammonium sulphate fractionation, ethanol precipitation, Sephadex G-200 gel filtration and DEAE-Sephadex column chromatography. 2. The purified preparation was free from beta-glucuronidase, beta-galactosidase, acid phosphatase, inorganic pyrophosphatase and adenosine 3'-phosphate 5'-sulphatophosphate sulphohydrolase activities. 3. Polyacrylamide-gel electrophoresis indicated that the purified preparation was not homogeneous. 4. Chicken brain arylsulphatase was markedly inhibited by carbonyl reagents in the presence of traces of Cu(2+) in the system. Other metal ions such as Fe(2+) and Zn(2+), were inactive. 5. Ascorbic acid alone had no effect on enzyme activity but enhances the inhibition by Cu(2+). 6. Chicken brain arylsulphatase A resembled arylsulphatase A of other animal species in its kinetic properties such as K(m) value, anomalous time-activity relationship and the inhibitory effect of phosphate, sulphite and sulphate ions. However, its electrophoretic mobility, behaviour under zinc acetate fractionation and stimulation by Ag(+) were similar to arylsulphatase B of other animal species. Thus, this enzyme did not correspond to either arylsulphatase A or arylsulphatase B but properties of both. 7. The purified enzyme preparation can degrade cerebroside 3-sulphate.
 ...
PMID:Purification and properties of arylsulphatase A from chicken brain. 507 33

Investigations were undertaken to study the role of lupeol, a pentacyclic triterpene from Crataeva nurvala stem bark, in calcium oxalate experimental rat urolithiasis. A 2% solution of ammonium oxalate was administered by gastric intubation for inducing hyperoxaluric condition in adult male rats of Wistar strain. The duration of treatment was for 15 days. This resulted in increased urinary excretion of oxalate associated with reduction in citrate and glycosaminoglycans. The urinary marker enzymes which indicate renal tissue damage namely--lactate dehydrogenase, inorganic pyrophosphatase, alkaline phosphatase, gamma glutamyl transferase, beta-glucuronidase and N-acetyl beta-D glucosaminidase were found to be elevated. Lupeol administration (25 mg/kg body weight/day) reduced significantly the renal excretion of oxalate. It also reduced the extent of renal tubular damage as evidenced from the decreased levels of the above enzymes in urine. Such a reduction is likely to be beneficial in minimizing the deposition of stone-forming constituents in the kidney which provides antilithic effect.
 ...
PMID:Effect of lupeol, a pentacyclic triterpene, on urinary enzymes in hyperoxaluric rats. 871 54

The aim of the work described in this paper was to characterize the tubers of potato (Solanum tuberosum var. Prairie) plants that had been transformed with the Escherichia coli ADPglucose pyrophosphorylase (EC 2.7.7.27) gene, glgC-16, under the control of a patatin promoter. Over 30 lines of transformed plants with increased ADPglucose pyrophosphorylase activity were obtained. The tubers of six of these lines were compared with those of control plants expressing the gene for beta-glucuronidase. The average increase in pyrophosphorylase activity was 200%, and the highest was 400%. Western immunoblotting of tuber extracts showed that the amounts of glgC-16 protein were linearly related to the extractable activity of the ADPglucose pyrophosphorylase. Cell fractionation studies showed that the increased activity of the pyrophosphorylase in the glgC-16 tubers had a similar intracellular location, the amyloplast fraction, to that found in the control tubers. No pleiotropic changes in the maximum catalytic activities of the following enzymes could be detected in the glgC-16 tubers: sucrose synthase, fructokinase, UDPglucose pyrophosphorylase, phosphofructokinase, soluble starch synthase, starch branching enzyme, phosphoglucomutase and alkaline inorganic pyrophosphatase. The glgC-16 tubers are held to be suitable for the study of the role of ADPglucose pyrophosphorylase in the control of starch synthesis.
 ...
PMID:Characterization of transgenic potato (Solanum tuberosum) tubers with increased ADPglucose pyrophosphorylase. 897 57