Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.2.1.21 (beta-glucosidase)
3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The optimal assay conditions and the levels of seven lysosomal glycohydrolases (alpha-D-galactosidase, beta-D-galactosidase, beta-D-glucosidase, beta-D-glucuronidase, beta-N-acetyl-D-glucosaminidase (2-acetamido-2-deoxy-beta-D-glucoside acetamidodeoxyglucohydrolase), alpha-D-mannosidase, alpha-L-fucosidase) were determined in human peripheral unseparated lymphocytes, T and non-T lymphocyte subpopulations. From fifteen adult volunteers the enzymes were assayed by fluorimetric procedures using the corresponding 4-methylumbelliferyl glycosides as substrates. The enzyme assay procedures displayed good precision and reproducibility. All the tested enzymes had higher activities in non-T than T lymphocytes. This difference was statistically highly significant, especially when the enzyme contents were expressed on a DNA, rather than mg protein, basis. Unseparated lymphocytes displayed levels of lysosomal enzymes which corresponded to the proportion of T and non-T lymphocytes in the unseparated preparation, indicating that the process of lymphocyte fractionation caused neither loss nor activation of lysosomal enzymes. It is concluded that the observed difference in lysosomal enzyme levels is an authentic imprint of the two lymphocyte subpopulations, implying a differential role played by the lysosomal apparatus in the same cells.
...
PMID:Lysosomal glycohydrolases in normal T and non-T peripheral lymphocytes. 660 89

Human tumor cells of neurectoderm origin contain a high proportion of alpha-L-fucosyl linkages were determined by high-resolution, 500-MHz, 1H-n.m.r. spectroscopy which gave signals characteristic for alpha-L-Fucp-(1 leads to 3)-D-GlcNAc residues these L-fucosyl residues. This was shown by use of a specific alpha-L-fucosidase from almond emulsin and a broad-spectrum alpha-L-fucosidase from rat testes. The exact alpha-L-fucosyl linkages were determined by high-resolution, 500-MHz, 1H-n.m.r. spectroscopy which gave signals characteristic for alpha-L-Fucp-(1 leads to 3)-D-GlcNAc residues linked to branches and for alpha-L-Fucp-(1 leads to 6)-D-GlcNAc residues linked to the core. More than 95% of the asparagine-linked GlcNAc residues were substituted with (1 leads to 6)-alpha-L-fucosyl groups. Further definition of the range of neutral glycopeptides was obtained with immobilized lectins. Binding to E-PHA-agarose suggested the presence of a beta-D-mannopyranosyl residue substituted at O-4 by a 2-acetamido-2-deoxy-D-glucopyranosyl group. alpha-L-Fucp-(1 leads to 3)-GlcNAc interfered with this binding since removal of alpha-L-fucosyl groups by almond emulsin alpha-L-fucosidase increased the binding by 100%. These studies demonstrate the ability of a combination of high-resolution 1H-n.m.r., enzyme degradation, and lectin-binding affinities to delineate structural elements of small amounts of oligosaccharide residues.
...
PMID:Characterization of the neutral glycopeptides containing the structure alpha-L-fucopyranosyl-(1 leads to 3)-2-acetamido-2-deoxy-D-glucose from human neuroblastoma cells. 662 47

The activities of various glycosidases in homogenates of the small intestinal mucosa of two adult and 18 suckling tammar wallabies (M. eugenii) aged from 6 to 50 weeks were investigated. Lactase (beta-D-galactosidase), beta-N-acetylglucosaminidase, alpha-L-fucosidase and neuraminidase activities were high during the first 34 weeks post partum and then declined to very low levels. Maltase, isomaltase, sucrase and trehalase activities were very low or absent during the first 34 weeks, and then increased. The lactase activity was unusual in being greater in the distal than the middle or proximal thirds of the intestine, and in its low pH optimum (pH 4.6), inhibition by p-chloromercuribenzene sulfonate but not by Tris, and lack of cellobiase activity. These properties are those of a lysosomal acid beta-galactosidase rather than of a brush border neutral lactase. The maltase activity had the characteristics of a lysosomal acid alpha-glucosidase early in lactation and of a brush border neutral maltase in adult animals. The significance of these findings is discussed in relation to changes in dietary carbohydrates during weaning and to the mode of digestion of milk carbohydrates by the pouch young.
...
PMID:Intestinal lactase (beta-galactosidase) and other glycosidase activities in suckling and adult tammar wallabies (Macropus eugenii). 678 21

The specific activities of several glycosidases (beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase) were determined in human sera from a control group to 10 normal subjects and in four groups, each of 10 patients, with acute viral hepatitis, acute pancreatitis, acute myocardial infarction and breast cancer. The results show significantly higher activities in acute viral hepatitis for beta-N-acetylglucosaminidase, beta-D-glucosidase and alpha-D-glucosidase (p less than 0.001); in acute pancreatitis for the first two of these enzymes (p less than 0.001); and in breast cancer for beta-D-glucosidase (p less than 0.001). Further, lower differences were found in the patients with acute viral hepatitis for beta-D-fucosidase and alpha-L-fucosidase (p less than 0.01); in acute myocardial infarction for beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase and beta-D-galactosidase (p less than 0.01, p less than 0.05, p less than 0.05, p less than 0.01 and p less than 0.01, respectively); and in breast cancer for beta-N-acetylglucosaminidase (p less than 0.01). No significant differences were found for the other glycosidases.
...
PMID:Serum beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase levels in acute viral hepatitis, pancreatitis, myocardial infarction and breast cancer. 680 Jun 74

Some hydrolytic enzyme activities, mainly typical of lysosomal localization, have been determined in blood sera from patients who ingested a rapeseed oil (denatured with anilines and treated by a thermal process), and in healthy subjects. beta-N-Acetylglucosaminidase, beta-D-glucosidase, beta-D-glucuronidase, alpha-L-fucosidase and leucine aminopeptidase activities were significantly higher when compared with controls (p less than 0.001); higher activities but not significant (p less than 0.2) differences were found for alpha-D-mannosidase and alkaline phosphatase. In contrast, beta-D-galactosidase, alpha-D-galactosidase, acid phosphatase and lipase showed lower activities than controls. The significance of these results is discussed.
...
PMID:Hydrolytic enzyme activities, mainly from lysosomal localization, in sera from patients who ingested a toxic oil. 683 4

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.
...
PMID:Clearance and binding of native and defucosylated lactoferrin. 688 70

To study the role of lysosomal enzymes in glomeruli, we examined specific activities of lysosomal hydrolases in isolated glomeruli and, for comparison in isolated tubules, from rat kidney cortex of normal animals and animals with puromycin aminonucleoside nephrosis (PAN). Nephrotic syndrome was induced in rats by a single intraperitoneal injection of aminonucleoside and the rats were sacrificed at the time of peak proteinuria. Colloidal iron staining of renal cortex demonstrated decreased staining for the epithelial polyanion in animals with PAN. Lysosomal enzymes were determined by fluorogenic and colorimetric methods. In normal kidney, total specific activities of cathepsin beta 1, beta-2-fucosidase, acetyl-beta-glucosaminidase, and arylsulfatase were lower in glomeruli compared with tubules and with tissue slices of the same kidney. Total activity of acid phosphatase was higher in glomeruli than tubules. In glomeruli of PAN rats, there were lower activities of N-acetyl-beta-glucosaminidase, D-fucosidase, beta-glucosidase, beta-glucoronidase, and arylsulfatase compared with control rats. Activity of acid phosphatase, on the other hand, was higher in glomeruli of PAN than control rats. All differences were statistically significant. These studies demonstrate that (1) activities of lysosomal enzymes in normal glomeruli and in glomeruli of nephrotic rats have a property distinct from the rest of the kidney, and (2) the specific activities of lysosomal hydrolases are altered in glomeruli of rats with PAN. These studies suggest that changes in activities of lysosomal enzymes may be related to pathogenesis of this glomerulopathy.
...
PMID:Activities of lysosomal enzymes in isolated glomeruli. Alterations in experimental nephrosis. 732 25

Fifty-six strains of lactobacilli were examined for the production of glycosidases and proteases (arylamidases) that could be associated with the ability to grow in vivo and/or be a factor in the pathogenesis of endocarditis. The strains were from seven species, with an emphasis on Lactobacillus rhamnosus and Lact. paracasei subsp. paracasei, both of which have been associated with endocarditis and provided 12 of the 13 strains isolated from cases of the disease. Other species were Lact. acidophilus, Lact. plantarum, Lact. salivarius, Lact. fermentum and Lact. oris. Commonly expressed glycosidase activities were alpha-D-galactosidase and beta-N-acetyl-D-glucosaminidase followed by beta-D-glucosidase and alpha-L-fucosidase. The combined production of beta-N-acetyl-D-glucosaminidase and alpha-D-galactosidase was a feature of the endocarditis isolates. In contrast, beta-D-galactosidase was produced by very few of the strains within species implicated in endocarditis but most of the strains of Lact. salivarius, Lact. fermentum and Lact. oris. The most commonly produced arylamidases active against substrates employed for testing human blood clotting cascade were activated protein C(Ca)-like, activated factor X(Xa)-like and Hageman factor-like followed by kallikrein-like and chymotrypsin-like enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Enzyme production by lactobacilli and the potential link with infective endocarditis. 769 50

Alterations in the activities of certain lysosomal enzymes such as beta-D-galactosidase, beta-D-glucosidase, beta-D-glucuronidase, alpha-L-fucosidase, N-acetyl-beta-D-glucosaminidase, cathepsins B and D were studied in serum and tissue homogenates of buccal mucosa of hamsters treated with 0.5%, 7,12-dimethylbenz[a]anthracene (DMBA) in liquid paraffin. Among the enzymes studied, the activities of beta-D-galactosidase and N-acetyl-beta-D-glucosaminidase showed significant elevation both in serum and tissue homogenates fro papilloma onwards and the elevations were progressive with the development of carcinomas. The elevations in the activities of alpha-D-fucosidase and cathepsin D were found to be significant from papillomatous tissue onwards whereas in serum they showed higher activities only in carcinoma stages. The activities of beta-D-glucosidase, beta-D-glucuronidase and cathepsin B in both serum and in tissue homogenate were elevated markedly only in carcinoma stages. It is suggested that beta-D-galactosidase and N-acetyl-beta-D-glucosaminidase may be used as diagnostic markers for premalignant and malignant lesions of oral mucosa.
...
PMID:Studies of the activities of lysosomal enzymes in serum and buccal pouch tissue of hamsters during 7,12-dimethylbenz[a]anthracene-induced carcinogenesis. 862 88

Nectrisine, discovered as an immunomodulator, was found to inhibit alpha-glucosidase, alpha- and beta-mannosidases, beta-glucosidase and beta-N-acetylglucosaminidase, in that order of inhibition strength. Beta-Galactosidase, alpha-fucosidase, and neuraminidase were insensitive to this antibiotic. Also sensitive was the trimming glucosidase I which participates in the first step of modifying N-glycosidic oligosaccharide. Nectrisine demonstrated an inhibitory effect at the cellular level as strong as expected based on its action at enzyme levels; castanospermine and 1-deoxynojirimycin did not. Nectrisine and castanospermine suppressed syncytium formation and hemolytic activity in Newcastle disease virus (NDV)-infected BHK cells, without blocking the synthesis and cell-surface expression of HANA glycoprotein of NDV.
...
PMID:Nectrisine is a potent inhibitor of alpha-glucosidases, demonstrating activities similarly at enzyme and cellular levels. 864 27


<< Previous 1 2 3 4 5 6 7 Next >>

---