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)

Composition of the aqueous phase of mammary secretions during the nonlactating and postpartum periods was determined in nine cows. Protein concentrations increased until several days before parturition and then declined precipitously. Lactose declined rapidly in early involution, remained low during the middle of the nonlactating period, and increased rapidly prepartum. The pH of secretions followed an inverse pattern to lactose and was negatively correlated with lactose during the nonlactating period but not the postpartum period. Peroxidase activity initially increased in secretions in early involution, then declined until parturition when peroxidase activity again increased. Activities of the glycosidic enzymes N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and alpha-mannosidase increased through the nonlactating period until 2 to 3 wk prepartum, from which time all three enzyme activities declined through the postpartum period. The magnitude of increase in the glycosidases was not the same; peak activity of N-acetyl-beta-D-glucosaminidase increased 20-fold over the activity at d 1 of involution, whereas beta-glucuronidase and alpha-mannosidase increased 4 to 5-fold over the same period.
 ...
PMID:Mammary function during the nonlactating period: enzyme, lactose, protein concentrations, and pH of mammary secretions. 357 23

1. The particulate form of lactating bovine mammary lactose synthetase activity is shown to be more highly organized than previously reported. 2. A novel method of shattering frozen mammary tissue with effective cell disruption is described. 3. The apparent subcellular distribution of lactose synthetase was shown to reflect the method of homogenization. 4. After mild homogenization particles associated with a high content of intact lactose synthetase activity sedimented in the lysosome size range between 5x10(4) and 3x10(5)g-min. 5. Lactose synthetase was dissociated and solubilized by VirTis homogenization and ultrasonic treatment. The activities and behaviour of UDP-galactose hydrolase, succinate dehydrogenase, beta-glucuronidase and phosphodiesterase I were compared. 6. Inhibition of UDP-galactose hydrolase by UTP and alpha-lactalbumin was observed.
 ...
PMID:The lactose synthetase particles of lactating bovine mammary gland. Preparation of particles with intact lactose synthetase. 430 May 6

1. The conditions that promoted the solubilization of particulate lactose synthetase were effective for solubilizing the thiamine pyrophosphatase of the Golgi apparatus but differed from those effective for beta-glucuronidase or acid phosphatase of lysosomes. 2. Lactose synthetase-containing particles did not bind Mg(2+) or Cs(+) ions, suggesting that they are not related to endoplasmic reticulum membranes. 3. Intact lactose synthetase and thiamine pyrophosphatase particles banded isopycnically at a density of 1.143 in a sucrose gradient. The dissociated ;A' sub-unit of lactose synthetase, UDP-galactose hydrolase, p-nitrophenyl phosphate acid phosphatase, alkaline phosphatase and phosphodiesterase I were associated with particles of a broad density range from 1.12 to 1.20. Lysosomal enzymes beta-glucuronidase, arylsulphatase and beta-glycerophosphate acid phosphatase were associated with particles of density 1.20, 1.175 and 1.15 respectively. 4. Rate-zonal sedimentation studies indicated that lactose synthetase particles have S(20,w) values exceeding 24000s, corresponding to spherical particles of diameter exceeding 5.4x10(-5)cm. 5. Electron micrographs of lactose synthetase particles purified over 20-fold revealed small spherical bodies (0.1-0.5mu) resembling lysosomes, the smaller of which were attached to membranes, and larger heterogeneous spherical or oval bodies (0.7-1.8mu) resembling lipofuscin secretory granules. 6. The relationship between lactose synthetase particles and the Golgi origin of secretion granules is discussed.
 ...
PMID:The lactose synthetase particles of lactating bovine mammary gland. Characteristics of the particles. 430 May 7

Weanling or adult (9 wk old) rats were fed diets containing 0, 250 or 500 g lactose/kg for 10 days, after which the activities of six caecal microbial enzymes (azoreductase, beta-glucosidase, beta-glucuronidase, nitrate reductase, nitroreductase and urease) were determined. Adult controls had larger caeca than weanlings, but the numbers of bacteria were not significantly different. Expressed in relation to body weight, caecal microbial enzyme activities were significantly lower in adult controls, with the exceptions of beta-glucuronidase and urease. Lactose caused caecal enlargement; this was greatest in weanling animals, which also showed a decreased concentration of bacteria. Lactose increased total nitrate reductase and urease activities in both age groups, but decreased total azoreductase and nitroreductase activities in weanlings. Enzyme activities per 10(9) bacteria were decreased for azoreductase, beta-glucosidase, beta-glucuronidase and nitroreductase in both age groups, while urease activity increased. Azoreductase and nitroreductase activities were highly correlated but nitrate reductase and urease did not correlate significantly with any other enzyme activity.
 ...
PMID:Dietary lactose and the metabolic activity of the caecal microfloras of weanling and adult rats. 642 83

Beta-glucuronidase is a lysosomal enzyme that plays an essential role in normal turnover of glycosaminoglycans and remodeling of the extracellular matrix components in both physiological and inflammatory states. The regulation mechanisms of enzyme activity and protein targeting of beta-glucuronidase have implications for the development of a variety of therapeutics. In this study, the effectiveness of various carbohydrate-immobilized adsorbents for the isolation of bovine liver beta-glucuronidase (BLG) from other glycosidases was tested. Beta-glucuronidase and contaminating glycosidases in commercial BLG preparations bound to and were coeluted from adsorbents immobilized with the substrate or an inhibitor of beta-glucuronidase, whereas beta-glucuronidase was found to bind exclusively with lactamyl-Sepharose among the adsorbents tested and to be effectively separated from other enzymes. Binding and elution studies demonstrated that the interaction of beta-glucuronidase with lactamyl-Sepharose is pH dependent and carbohydrate specific. BLG was purified to homogeneity by lactamyl affinity chromatography and subsequent anion-exchange high-performance liquid chromatography (HPLC). Lactose was found to activate beta-glucuronidase noncompetitively, indicating that the lactose-binding site is different from the substrate-binding site. Binding studies with biotinyl glycoproteins, lipids, and synthetic sugar probes revealed that beta-glucuronidase binds to N-acetyllactosamine/lactose-containing glycoconjugates at neutral pH. The results indicated the presence of N-acetyllactosamine/lactose-binding activity in BLG and provided an effective purification method utilizing the novel carbohydrate binding activity. The biological significance of the carbohydrate-specific interaction of beta-glucuronidase, which is different from the substrate recognition, is discussed.
 ...
PMID:Novel carbohydrate-binding activity of bovine liver beta-glucuronidase toward lactose/N-acetyllactosamine sequences. 1677 8