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

A procedure was developed for the analytical isolation of brush border and basal lateral plasma membranes of intestinal epithelial cells. Brush border fragments were collected by low speed centrifugation, disrupted in hypertonic sorbitol, and subjected to density gradient centrifugation for separation of plasma membranes from nuclei and core material. Sucrase specific activity in the purified brush border plasma membranes was increased fortyfold with respect to the initial homogenate. Basal lateral membrane were harvested from the low speed supernatant and resolved from other subcellular components by equilibrium density gradient centrifugation. Recovery of Na, K-ATPase activity was 94%, and 61% of the recovered activity was present in a single symmetrical peak. The specific activity of Na, K-ATPase was increased twelvefold, and it was purified with respect to sucrase, succinic dehydrogenase, NADPH-cytochrome c reductase, nonspecific esterase, beta-glucuronidase, DNA, and RNA. The observed purification factors are comparable to results reported for other purification procedures, and the yield of Na, K-ATPase is greater by a factor of two than those reported for other procedures which produce no net increase in the Na, K-ATPase activity. Na, K-ATPase rich membranes are shown to originate from the basal lateral plasma membranes by the patterns of labeling that were produced when either isolated cells or everted gut sacs were incubated with the slowly permeating reagent 35S-p-(diazonium)-benzenesulfonic acid. In the former case subsequently purified Na, K-ATPase rich and sucrase rich membranes are labeled to the same extent, while in the latter there is a tenfold excess of label in the sucrase rich membranes. The plasma membrane fractions were in both cases more heavily labeled than intracellular protein. Alkaline phosphatase and calcium-stimulated ATPase were present at comparable levels on the two aspects of the epithelial cell plasma membrane, and 25% of the acid phosphatase activity was present on the basal lateral membrane, while it was absent from the brush border membrane. Less than 6% of the total Na, K-ATPase was present in brush border membranes.
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PMID:Analytical isolation of plasma membranes of intestinal epithelial cells: identification of Na, K-ATPase rich membranes and the distribution of enzyme activities. 13 16

56 human liver biopsy specimens with insignificant or no histological changes, but with abnormally strong canalicular alkaline phosphatase activity, were studied histochemically for other enzyme changes. In comparison with normal specimens, more extensive and increased canalicular activity of gamma-glutamyl transferase, and increase of canalicular leucine aminopeptidase, was found, while the sinusoidal activity of the latter enzyme was decreased. Staining for adenosine triphosphatase regularly desclosed the normal pattern of sinusoidal and canalicular activity. The lysosomal enzymes, acid phosphatase and beta-glucuronidase, stained more intensely than ordinarily, while the reactions for enzymes present in the cytosol (lactic dehydrogenase), in the mitochondria (succinic dehydrogenase, imonoamine oxidase) and in the endoplasmic reticulum (glucose-6-phosphatase) were normal.
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PMID:On histochemical enzyme changes in association with canalicular activity of alkaline phosphatase in human liver. 24 Dec 3

The liver affection in acute experimental pancreatitis (AEP) could be reflected by changes of enzymatic activity in the liver and in serum. The histoenzymatic studies of the liver of dogs with AEP of different severity and time of duration induced according to Elliott's method were performed and the constellation of serum enzymatic activities considering treatment with prostacyclin was estimated. The histoenzymatic reactions on succinic dehydrogenase, lactic dehydrogenase and alkaline phosphatase were depressed with progression of time and severity of AEP. In contrast, the reaction on acid phosphatase was augmented at the same time. Serum AspAT, AlAT and alkaline phosphatase were augmented in the later phase of AEP, but acid phosphatase and beta-glucuronidase were not significantly changed. The treatment with PGI2 limited both histoenzymatic reactions and alterations of serum enzymatic activities. These results support the significance of changes in enzymatic activities in the course of liver reaction on pancreatogenic noxa during acute pancreatitis, and suggest the protective effect of PGI2 against liver injury in this disease.
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PMID:The enzymatic studies of the liver in acute experimental pancreatitis in dogs treated with prostacyclin (PGI2). 329 21

Phagocytic vesicles were obtained by density gradient centrifugation of homogenized rabbit alveolar macrophages that had ingested emulsified paraffin oil contained Oil Red O. The phagocyte vesicles floated and thereby were separated from the soluble fraction and from other cell components which sedimented. The purity of the isolated vesicles was documented by electron microscopy, chemical and enzyme analysis. The vesicles contained 87% of the cell-associated Oil Red O, and were essentially free of DNA, RNA, succinic dehydrogenase, and glucose-6-phosphatase. Acid phosphatase, beta-glucuronidase, and catalase were transferred from the sedimenting fraction to the phagocytic vesicle fraction during phagocytosis, whereas enzyme activities of the soluble fraction remained unchanged. Half of the catalase of resting macrophages was in the pellet fraction and, compared with acid phosphatase, greater amounts of digitonin were required to release full activity. Such differential latency has been described for enzymes of peroxisomes vs. those of lysosomes. Compared with polymorphonuclear leukocyte vesicles studied previously, phagocytic vesicles of macrophages had more electron-dense material and lower Oil Red O:protein, phospholipid:protein, and enzyme:protein ratios. It is thus probable that secondary lysosomes become part of the macrophage vesicle. When paraffin oil particles, the stimulus for phagocytic vesicle formation, were washed away from the macrophages, acquisition of hydrolases by preformed vesicles ceased, i.e. transfer of these enzymes into phagocytic vesicles occurred only during or shortly after the formation of new vesicles. As noted previously by others, the content of acid hydrolases of stimulated alveolar macrophages was doubled in comparison to normal cells. The difference between stimulated and normal macrophages was even more marked when isolated phagocytic vesicles were analyzed. Vesicles from stimulated macrophages had 3-5 times more enzyme activity (per milligram of vesicle protein or per amount of paraffin oil ingested) than did vesicles from normal cells.
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PMID:Isolation and properties of phagocytic vesicles. II. Alveolar macrophages. 501 Nov 3

Epithelial-cell enriched primary cultures have been established from rat ventral prostate (RVP). Minced ventral prostates were dissociated with 0.5% collagenase in F12K tissue culture medium containing 1% fetal bovine serum. This treatment resulted in the gradual removal of stromal elements from the base of the epithelial cells. After 60 minutes of digestion the aggregates of epithelial cells were washed and plated at high density in F12K plus 10% horse serum. After 48 hours in vitro the unattached cells were removed from the culture dishes, washed, and reinoculated into new culture vessels containing fresh medium. After 96 hours in vitro, the aggregates had attached to the culture vessels and spread out to yield discrete patches of epithelial cells. By 144 hours in vitro the patches of cells had grown and coalesced to form a semi-confluent monolayer of epithelial cells. Ultrastructrual examination of these cultures indicated that adjacent cells were joined by desmosomes and tight junctions and had formed "lumen-like structures" into which projected microvilli. In addition, the cells contained secretory granules and tonofilaments, giving them a morphological appearance similar to prostate epithelial cells in the intact organ. The primary cultures also retained histochemical activities for acid phosphatase, beta-glucuronidase, and succinic dehydrogenase that were similar to the intact organ.
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PMID:Isolation, culture and characterization of epithelial cells derived from rat ventral prostate. 625 35

Human mammary tumours were grown in diffusion chambers in the heterologous host--Charle's Foster rat. The effect of oophorectomy-induced alterations of the hormonal environment of the host in breast tumour cells grown in the diffusion chamber were studied with respect to their growth patterns and enzymatic characteristics. The tumour cells not only survived but actively proliferated as indicated by the increase in cell count and formation of cell sheets as well as by the presence of mitotic figures. Cytochemical studies of certain enzymatic activities, i.e. succinic dehydrogenase, alkaline phosphatase, acid phosphatase and beta-glucuronidase indicate--except for a slight depression of the overall activity--that the distribution patterns are more or less maintained following diffusion chamber culture. The alteration of the hormonal environment by oophorectomy influences the cell growth and the enzymatic activity of the human tumour cells inside the diffusion chambers. The results clearly indicate that D.C. culture technique provides a useful method for assessment of growth and hormonal responsiveness of human tumours.
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PMID:Studies on growth and enzymatic characteristics of human mammary tumours grown in heterologous host. 668 51

Adult male rats receiving styrene by gavage (200 or 400 mg kg-1, 6 days a week) for 100 days exhibited a significant dose-dependent increase in hepatic benzo[a]pyrene hydroxylase and aminopyrine-N-demethylase, a decrease in glutathione-S-transferase and no change in glucose-6-phosphatase. A decrease in the activity of mitochondrial succinic dehydrogenase and beta-glucuronidase was also observed. Activity of acid phosphatase was decreased only at the higher dose level. Levels of serum glutamic oxaloacetic transaminase and glutamic pyruvic transaminase were elevated only at the higher dose level. The absolute and relative weights of the liver of control and treated animals showed no significant difference. Histopathological studies of the liver tissue revealed tiny areas of focal necrosis, consisting of few degenerated hepatocytes and inflammatory cells at the higher dose level only.
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PMID:Hepatic effects of orally administered styrene in rats. 718 5

The sdhB gene encoding an iron-sulfur (Ip) subunit of succinate dehydrogenase (SDH, EC 1.3.99.1) complex was cloned from Mortierella alpina 1S-4. The deduced amino acid sequence of SdhB from M. alpina 1S-4 showed high similarity to those of SdhB from other organisms. The mutated sdhB (CBXB) gene encodes a modified SdhB with an amino-acid substitution (a highly conserved histidine residue within the third cysteine-rich cluster of SdhB replaced by a leucine residue) and is known to confer carboxin resistance. We succeeded in transforming M. alpina 1S-4 by using the CBXB gene as a selectable marker gene and expressing the heterologous uidA gene encoding beta-glucuronidase of Escherichia coli. Moreover, transformation efficiency was up to 40-50 transformants per 4.0 x 10(8) spores. This carboxin-transformation system, characterized by marginal background growth and mitotic stability in M. alpina 1S-4, is considered to be widely useful for the wild strain, M. alpina 1S-4, and various derivative mutants without laborious preparation of auxotrophic mutants as a host strain.
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PMID:Transformation of an oleaginous zygomycete Mortierella alpina 1S-4 with the carboxin resistance gene conferred by mutation of the iron-sulfur subunit of succinate dehydrogenase. 1946 16