Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Rabbit beta-glucuronidase. Subcellular distribution and immunochemical properties.

ABSTRACT: 1. The subcellular distribution of beta-glucuronidase and other hydrolases in rabbit liver was investigated. beta-Glucuronidase was found in both microsomal and lysosomal fractions. 2. Multiple forms of beta-glucuronidase were present in extracts of microsomal and lysosomal fractions. All forms were common to both fractions. 3. A specific antiserum against beta-glucuronidase was raised, and characterized by immunoprecipitation and affinity-chromatography procedures. 4. The immunological identity of the multiple forms in the pure beta-glucuronidase preparation, and the immunological identity of the beta-glucuronidase complement of lysosomal extracts with that of microsomal extracts, were demonstrated by means of the antiserum. The presence of inactive enzyme in various enzyme preparations was shown.

SUBMITTER: Dean RT

PROVIDER: S-EPMC1166226 | biostudies-other | 1974 Mar

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

Rabbit beta-glucuronidase. Purification and properties, and the existence of multiple forms.

Project description:1. beta-Glucuronidase (EC 3.2.1.31) was purified from rabbit liver by a procedure involving autolysis, (NH(4))(2)SO(4) fractionation, chromatography on DEAE-cellulose and hydroxyapatite, gel filtration, sedimentation in a sucrose gradient, and isoelectric focusing. 2. Electron microscopy revealed ferritin as the major contaminant in later stages of purification and also showed aggregates of enzyme molecules. Particular attention was paid to the removal of ferritin. 3. The purified enzyme was homogeneous in polyacrylamide-gel electrophoresis both in non-dissociating conditions and in the presence of sodium dodecyl sulphate, and in Ouchterlony gel diffusion and immunoelectrophoresis against polyspecific antisera. 4. Sedimentation in sucrose gradients gave a molecular weight of 300000, whereas gel filtration indicated 440000. 5. Subunits of 75000 molecular weight were observed in gel electrophoresis in the presence of sodium dodecyl sulphate and in gel filtration in the presence of urea. 6. The K(m) value for p-nitrophenyl beta-d-glucuronide was 0.6mm, and the enzyme was extremely sensitive to lactone inhibitors. It was also inhibited by Hg(2+) ions. 7. Multiple forms were observed in the pure enzyme by isoelectric focusing, with pI values of 4.5-5.8. Subunits showed similar heterogeneity. The origin of the multiple forms was investigated in detail, and the possibility of artifact generation largely excluded. Some of the forms of lowest pI disappeared after neuraminidase digestion. The nature of the residual heterogeneity remains to be elucidated.

| S-EPMC1166225 | biostudies-other

Distribution and gene mutation of enteric flora carrying β-glucuronidase among patients with colorectal cancer.

Project description:ObjectiveTo explore the difference of distribution in intestinal flora among colorectal cancer patients and healthy controls and investigate characteristics and changes of sequences in beta-glucuronidase (β-glucuronidase, β-G).MethodsBacterial genomic DNA and E. coli DNA in feces were extracted from colorectal cancer patients and healthy controls respectively. Specific primers for β-G gene were designed and amplified by PCR as templates of fecal bacteria genomic DNA and E. coli DNA respectively.ResultsCompared with normal control, the amount of E. coli in cancer group increased significantly, Lactobacillus and Bifidobacterium probiotics reduced significantly, and proportional quantity of anaerobic bacteria and aerobic bacteria reversed. The intestinal flora carry β-G in both groups, and homologies with uidA gene sequences encoding the β-G were 99% and 98% respectively. In colorectal cancer group the 1141th and 1148th A base were deleted. The 1149th A base mutated into T base, and the 1158th bit A base mutated into G base; however, in healthy control group the 1141th and 1148th position A base was deleted, and the 1149th A base mutated into T base.ConclusionThere are differences of intestinal flora distribution between cancer group and healthy control group. The gene mutation and deletion of intestinal flora of β-G gene appear at the same time at 1141th, 1148th and 1149th in both cancer group and healthy control group, and 1158th genetic mutation appears only in colon cancer group.

| S-EPMC4483899 | biostudies-literature

Subcellular Distribution of Thyroid Hormone Receptor Beta in Ovarian Cancer.

Project description:Since the most well-known function of thyroid hormone receptors (TRs) relies on their ability to act as ligand-activated transcription factors, their subcellular localization has been recognized to be relevant for their biological meaning. The current study aimed to determine the prevalence and subcellular distribution of TR beta and TR beta-1 in ovarian cancer (OC). Tissue was collected from 153 patients that had undergone surgery due to OC at the Department of Obstetrics and Gynaecology of the Ludwig-Maximilians-University Munich. Immunohistochemistry detecting TR beta and TR beta-1 was performed. Staining signals were quantified and tested for association with clinico-pathological parameters including overall survival (OS). The subcellular distribution of TR beta and TR beta-1 differed among histologic subtypes, grade and FIGO stage. TR beta positivity was strongly linked to shortened overall survival (p < 0.001). Strikingly, this shortened OS was mainly attributed to those cases showing complete (p = 0.005) or incomplete shift of TR beta to the cytoplasm (p < 0.001). Significance was lost in multivariate testing. Cytoplasmatic localization of TR beta was associated with reduced OS, at least in univariate analysis. Since TRs have long been supposed to mainly function via the regulation of gene transcription in the nucleus, cytoplasmatic shifting might be interpreted as a regulator of their activity.

| S-EPMC8910424 | biostudies-literature

Phenoxyacetohydrazide Schiff bases: β-glucuronidase inhibitors.

Project description:Phenoxyacetohydrazide Schiff base analogs 1-28 have been synthesized and their in vitro β-glucouoronidase inhibition potential studied. Compounds 1 (IC50=9.20±0.32 µM), 5 (IC50=9.47±0.16 µM), 7 (IC50=14.7±0.19 µM), 8 (IC50=15.4±1.56 µM), 11 (IC50=19.6±0.62 µM), 12 (IC50=30.7±1.49 µM), 15 (IC50=12.0±0.16 µM), 21 (IC50=13.7±0.40 µM) and 22 (IC50=22.0±0.14 µM) showed promising β-glucuronidase inhibition activity, better than the standard (D-saccharic acid-1,4-lactone, IC50=48.4±1.25 µM).

| S-EPMC6271590 | biostudies-literature

Separation and properties of beta-galactosidase, beta-glucosidase, beta-glucuronidase and N-acetyl-beta-glucosaminidase from rat kidney.

Project description:1. The activities of beta-galactosidase, beta-glucosidase, beta-glucuronidase and N-acetyl-beta-glucosaminidase from rat kidney have been compared when 4-methylumbelliferyl glycosides are used as substrates. 2. Separation by gel electrophoresis at pH7.0 indicated slow- and fast-moving components of rat-kidney beta-galactosidase. 3. The fast-moving component is also associated with the total beta-glucosidase activity and inhibition experiments indicate that a single enzyme species is responsible for both activities. 4. DEAE-cellulose chromatography and filtration on Sephadex gels suggests that the beta-glucosidase component is a small acidic molecule, of molecular weight approx. 40000-50000, with optimum pH5.5-6.0 for beta-galactosidase and beta-glucosidase activities. 5. The major beta-galactosidase component has low electrophoretic mobility, a calculated molecular weight of 80000 and optimum pH3.7.

| S-EPMC1270276 | biostudies-other

Subcellular distribution of RNAs in HeLa cells

Project description:HeLa cells were fractioned in nucleus and cytoplasm to investigate the subcellular distribution of lncRNAs. Two-condition experiment, nuclear fraction vs. cytoplasmatic fraction from HeLa cells. Biological replicates: 2 with dye-swap

2015-06-30 | E-GEOD-62985 | biostudies-arrayexpress

Phosphatidylserine subcellular distribution and functions

Project description:Develop the organelle specific phosphatidylserine sensor to observe its distribution and stady its functions

2023-10-10 | PXD046019 |

Lysosomal β-glucuronidase regulates Lyme and rheumatoid arthritis severity.

Project description:Lyme disease, caused by the spirochete Borrelia burgdorferi, is the most prevalent arthropod-borne illness in the United States and remains a clinical and social challenge. The spectrum of disease severity among infected patients suggests that host genetics contribute to pathogenic outcomes, particularly in patients who develop arthritis. Using a forward genetics approach, we identified the lysosomal enzyme β-glucuronidase (GUSB), a member of a large family of coregulated lysosomal enzymes, as a key regulator of Lyme-associated arthritis severity. Severely arthritic C3H mice possessed a naturally occurring hypomorphic allele, Gusbh. C57BL/6 mice congenic for the C3H Gusb allele were prone to increased Lyme-associated arthritis severity. Radiation chimera experiments revealed that resident joint cells drive arthritis susceptibility. C3H mice expressing WT Gusb as a transgene were protected from severe Lyme arthritis. Importantly, the Gusbh allele also exacerbated disease in a serum transfer model of rheumatoid arthritis. A known GUSB function is the prevention of lysosomal accumulation of glycosaminoglycans (GAGs). Development of Lyme and rheumatoid arthritis in Gusbh-expressing mice was associated with heightened accumulation of GAGs in joint tissue. We propose that GUSB modulates arthritis pathogenesis by preventing accumulation of proinflammatory GAGs within inflamed joint tissue, a trait that may be shared by other lysosomal exoglycosidases.

| S-EPMC3871255 | biostudies-literature

Subcellular distribution of RNAs in HeLa cells

Project description:HeLa cells were fractioned in nucleus and cytoplasm to investigate the subcellular distribution of lncRNAs.

2015-06-30 | GSE62985 | GEO

Subcellular distribution and properties of kynurenine transaminase in rat liver.

Project description:Kynurenine transaminase activity in rat liver was found in both the mitochondrial and supernatant fractions. The mitochondrial and supernatant fractions contained (a) kynurenine-pyruvate transaminase, which showed a preference for pyruvate as amino acceptor and a pH optimum between 8.0 and 8.5, and (b) kynurenine-alpha-oxoglutarate transaminase, with a preference for alpha-oxoglutarate and a pH optimum between 6.0 and 6.5. Possible roles of these enzymes in tryptophan metabolism in the liver are discussed.

| S-EPMC1168385 | biostudies-other

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data