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)

A panel of 42 rodent x cat somatic cell hybrids has been used to assign seven structural genes for lysosomal enzymes to specific chromosomes in the domestic cat. The assignments include alpha-glucosidase (GANAB) to chromosome D1, alpha-galactosidase (GLA) to the X chromosome, beta-galactosidase 1 (GLB1) to chromosome B3, beta-glucuronidase (GUSB) to chromosome E3, alpha-mannosidase A (MANA) to chromosome B3, alpha-L-fucosidase (FUCA) to chromosome C1, and hexosaminidase A (HEXA) to chromosome B3. In all cases, the feline lysosomal enzyme genes were located in linkage groups which were syntenic with their homologous positions in the human gene map. These assignments expand the genetic map of the cat and reaffirm the extensive syntenic homology between the chromosome maps of man and cat.
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PMID:Chromosomal mapping of lysosomal enzyme structural genes in the domestic cat. 322 Apr 74

A simple, automated colorimetric microassay system has been designed to quantitate enzyme activities commonly used as markers for subcellular compartments. This system relies on the spectrophotometric reading of microtiter wells containing the chromophore products. The microassay allows rapid, economical, and quantitative analysis of enzyme activities associated with sucrose or Percoll gradient fractions used for subcellular fractionation studies as well as the screening of a large number of fractions derived from HPLC and other separation columns used for enzyme purification. We describe its use for the quantitation of activities associated with acid and alkaline phosphatases, alkaline phosphodiesterase, beta-glucuronidase, alpha-N-acetylglucosaminidase, alpha-mannosidase, alpha-L-fucosidase, glycosidases, serine esterases, and succinate dehydrogenase, and give the range of their sensitivities. This microassay system has been applied to the isolation of granules of cytolytic lymphocytes and to the identification and purification of a serine esterase from the isolated granules of these cells.
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PMID:Analysis of enzymatic activities of subcellular and chromatographic fractions by an automated colorimetric microassay system. 349 54

The enzyme activities of acid phosphatase, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, and alpha-D-mannosidase were not significantly different in patients with myopia, retinal detachment, hereditary macular dystrophy, and unusual progressive cone dystrophy. alpha-L-Fucosidase activity in sera was lower in three patients with myopia and in two patients with unusual progressive cone dystrophy than in most of the others. Leukocytic alpha-L-fucosidase activity was lower in those with unusual progressive cone dystrophy. The two unrelated patients with unusual progressive cone dystrophy had slowly deteriorating visual acuity, color vision, and photopic electroretinographic responses, but ophthalmoscopically normal fundi and noncontributory family histories.
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PMID:Progressive cone dystrophy associated with low alpha-L-fucosidase activity in serum and leukocytes. 401 93

The activities of six glycosidases in a rat colorectal adenocarcinoma were measured and compared with those of normal colonic mucosa. The specific activities of beta-galactosidase (EC 3.2.1.23) and beta-glucuronidase (EC 3.2.1.31) in the adenocarcinoma were similar to those of the corresponding ones in the normal mucosa, whereas those of beta-N-acetylglucosaminidase (EC 3.2.1.30), alpha-L-fucosidase (EC 3.2.1.51), alpha-galactosidase (EC 3.2.1.22) and beta-glucosidase (EC 3.2.1.21) were reduced in the former as compared with those in the latter. In the case of alpha-L-fucosidase, two forms were newly detected in the tumor. The relative abundance of three forms of beta-N-acetylglucosaminidase was quite different between the adenocarcinoma and the normal mucosa, and the level of the intermediate form in the tumor was markedly reduced. However, thermostability and Km values of two forms A and B in the tumor were not different from those of the corresponding ones in the normal tissue.
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PMID:Alteration in glycosidases from well-differentiated colorectal adenocarcinoma of rat. 404 71

In the newborn lamb, activities of lysosomal enzymes are lower in the duodenum and jejunum than in the ileum. In contrast, there are only minor differences, if any, in activities of lysosomal enzymes between the regions of the small intestine of 5-day-old lambs. In the duodenum, jejunum and ileum, activities of hexosaminidase, alpha-mannosidase, beta-mannosidase, alpha-L-fucosidase and phosphodiesterase are greater in newborn than in 5-day-old lambs. Only in the distal part of the small intestine are activities of beta-glucuronidase, alpha-glucosidase, alpha-galactosidase, beta-galactosidase, acid phosphatase and cathepsin B higher in the newborn than in 5-day-old lambs. Cathepsin B activity is lower in the duodenum and jejunum of the newborn than in 5-day-old lambs.
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PMID:Lysosomal enzymes in the intestine of the newborn lamb. 609 93

The following enzymes of lysosomal origin were fluorimetrically determined in maternal plasma from the second to the ninth month of pregnancy at 1-mth intervals: beta-D-N-acetylglucosaminidase (EC 3.2.1.30), beta-D-glucuronidase (EC 3.2.1.31), beta-D-glucosidase (EC 3.2.1.21), beta-D-galactosidase (EC 3.2.1.22), alpha-D-galactosidase (EC 3.2.1.23), alpha-L-fucosidase (EC 3.2.1.51) and alpha-D-mannosidase (EC 3.2.1.24) (pH 4.0). As reference microsomal alpha-D-mannosidase (pH 5.7) was also studied. Thirty-eight healthy women, aged 18-37 yr, who had a normal pregnancy followed by normal parturition, were studied. All enzymes, with the only exception of beta-D-galactosidase, showed a progressive and statistically significant increase of activity throughout pregnancy. At the end of pregnancy, the increase ranged from a maximum of 5.6-fold for beta-D-N-acetylglucosaminidase to a minimum of 0.55-fold for alpha-D-mannosidase, pH 5.7. In the case of beta-D-N-acetylglucosaminidase, the level at the fifth month of pregnancy was significantly higher than that at the third month, and from the sixth to the ninth month each level significantly differed from that of the month immediately preceding.
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PMID:Behaviour of several enzymes of lysosomal origin in human plasma during pregnancy. 609 42

The total protein content and the activities of lysosomal hydrolases (arylsulphatase, alkaline and acid phosphatases, beta-glucuronidase, beta-N-acetylhexosaminidase, alpha-L-fucosidase and beta-galactosidase) in the uteri of ovariectomized rabbits treated with different concentrations of progesterone, oestradiol-17 beta and a combination of progesterone and oestradiol were determined. The enzyme activities were also measured in the reproductive organs of rabbits induced to superovulate by PMSG and hCG. In superovulated and steroid-treated rabbits, the changes in lysosomal hydrolases were more obvious in the endometrium than the myometrium. Except for the myometrial alkaline phosphatase and beta-galactosidase and the endometrial alkaline phosphatase, there were no significant changes in the solubilities of hydrolases after treatment with steroids. beta-Galactosidase levels were significantly higher in the ovariectomized rabbits treated with progesterone. An antagonistic effect of oestradiol and progesterone was observed with respect to uterine weight, protein content and enzyme activities in the ovariectomized rabbits treated simultaneously with oestradiol and progesterone.
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PMID:Hormonal regulation of lysosomal hydrolases in the reproductive tract of the rabbit. 622 Jan 45

The localization of acid hydrolases was examined in Chinese hamster ovary cells with defective mannose 6-phosphate receptors; these mutants had been shown to exhibit reduced uptake and altered binding of exogenously added acid hydrolase (Robbins, A. R., Myerowitz, R., Youle, R. J., Murray, G. J., and Neville, D. M., Jr. (1981) J. Biol. Chem. 256, 10618-10622). Cells were grown in the presence of [3H]mannose, alpha-L-iduronidase and beta-hexosaminidase were immunoprecipitated sequentially, electrophoresed on polyacrylamide gels containing sodium dodecyl sulfate, and detected by fluorography. About 55% of the alpha-L-iduronidase and beta-hexosaminidase synthesized by the mutants in 12 h was found in the growth medium; parental cells secreted only approximately 15%. The mutants also secreted 2 to 6 times more alpha-mannosidase, beta-glucuronidase, and alpha-L-fucosidase than the parent as determined by measurements of enzyme activity. Intracellular levels of these enzymes were reduced in the mutants. The mutants secreted acid hydrolases in the precursor forms, within the cells these enzymes resided in lysosomes and were processed normally; thus, the mutants appeared aberrant only with respect to distribution of hydrolases between intracellular and extracellular compartments. [35S]methionine-labeled beta-hexosaminidase and alpha-L-iduronidase secreted by the mutants were taken up normally by both human fibroblasts and wild type CHO cells, and this uptake was inhibited by mannose 6-phosphate. Thus, the elevated secretion of acid hydrolases was not due to alteration of the mannose 6-phosphate recognition marker on the enzymes, but appears to result from alterations in the mannose 6-phosphate receptor.
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PMID:The mannose 6-phosphate receptor of Chinese hamster ovary cells. Compartmentalization of acid hydrolases in mutants with altered receptors. 627 Jan 23

The beta-N-acetylhexosaminidase, beta-glucuronidase, alpha-galactosidase, beta-galactosidase and alpha-L-fucosidase activities, in six different species of molluscs, have been studied. The optimum pH was acid in all cases, in agreement with the lysosomal origin of these enzymes. They generally show several pI in their isoelectrofocusing profiles. Kinetic studies with enzymes having several activities in one protein, i.e. beta-N-acetylhexosaminidase and beta-galactosidase, have been carried out with mixed substrates in order to determine the occurrence of several active sites. The action of these enzymes on glycosidic rests containing natural substrates has been studied by enzymatic hydrolysis.
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PMID:[Glycosidases of various mollusks: general properties, kinetic studies and action on natural substrates]. 629 19

Castanospermine (1,6,7,8-tetrahydroxyoctahydroindolizine) was tested against a variety of commercially available glycosidases and found to be a potent inhibitor of almond emulsin beta-glucosidase, and also to inhibit fungal beta-xylosidase. This alkaloid was inactive on yeast alpha-glucosidase, alpha- or beta-galactosidase, alpha-mannosidase, beta-N-acetylhexosaminidase, beta-glucuronidase, alpha-L-fucosidase. Fifty-percent inhibition of beta-glucosidase required about 10 micrograms/ml of castanospermine. The amount of inhibition was uniform throughout the time course, and the inhibition with regard to substrate concentration (p-nitrophenyl-beta-D-glucopyranoside) appeared to be of the mixed type. Castanospermine was also a potent inhibitor of beta-glucocerebrosidase when assayed with fibroblast extracts using either a fluorimetric or a radioactive assay. Interestingly enough, castanospermine also inhibited the lysosomal alpha-glucosidase, and this inhibition required comparable levels of alkaloid to that required for inhibition of beta-glucocerebrosidase. However, a number of other lysosomal glycosidases were not sensitive to castanospermine (i.e., alpha- or beta-galactosidase, alpha- or beta-mannosidase, alpha- or beta-L-fucosidase, beta-N-acetylhexosaminidase, beta-glucuronidase).
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PMID:Castanospermine, a tetrahydroxylated alkaloid that inhibits beta-glucosidase and beta-glucocerebrosidase. 640 22


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