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

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Query: EC:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the large granule fraction of rat liver, the density distribution of inhibitor-sensitive neutral ribonuclease is similar to that for acid hydrolases and its density distribution is similarly modified by Triton WR-1339 accumulation in lysosomes. Particulate neutral ribonuclease is latent; the enzyme is unmasked by very low digitonin concentrations or hypoosmotic shock. These observations demonstrate that the bulk of liver neutral ribonuclease is associated with the lysosomal system. In view of the neutral pH optimum of the enzyme and of some particularities of its distribution in fractionation experiments, the possiblilty of an extrahepatic origin of neutral ribonuclease has been investigated. After partial pancreatectomy, a significant decrease is observed in both plasma and liver neutral ribonuclease. The effect is specific, for it does not occur for other lysosomal enzymes. Also, labelled bovine pancreatic ribonuclease, when injected intravenously, is taken up by the liver. The sedimentable labelled enzyme has a density distribution similar to the distribution of other foreign proteins, horseradish peroxidase or yeast invertase. These results are explained by the uptake of plasmatic neutral ribonuclease from pancreatic origin by the liver.
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PMID:Hepatic nucleases. Extrahepatic origin and association of neutral liver ribonuclease with lysosomes. 0 Dec 73

Teratocarcinoma stem cells maintained in the undifferentiated state express a carbohydrate-binding component that recognizes oligomannosyl residues. This cell surface molecule is detected by a rosetta assay in which the stem cells form rosettes with glutaraldehyde-fixed trypsinized rabbit erythrocytes. Addition of simple sugars to the assay mixture has little effect, but rosette formation is inhibited by a series of mannose-rich glycoproteins (yeast invertase, yeast mannans and horseradish peroxidase). Periodate oxidation eliminates the inhibitory activity of invertase whereas pronase digestion has little effect, indicating that carbohydrate moieties are essential for inhibition. Invertase and its glycopeptide derivatives also inhibit the reaggregation of dispersed stem cells and promote the dissociation of preformed aggregates. These results suggest that intercellular adhesion of teratocarcinoma stem cels may be the consequence of the interaction of a lectin-like component detected in the rosette assay with a complementary oligosaccharide receptor on adjacent cells.
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PMID:Teratocarcinoma stem cells have a cell surface carbohydrate-binding component implicated in cell-cell adhesion. 47 26

Glycoproteins immobilized on membranes can be detected with high selectivity and sensitivity by the four-step procedure described in this work. The glycoproteins are first oxidized by sodium periodate and then polyacrylic polyhydrazides are coupled to the aldehyde groups generated in the sugar part of the glycoproteins. In the third step, a glycoenzyme, such as horseradish peroxidase, is coupled to the remaining hydrazide groups on the polymer through the aldehydes formed in its glycan chains. In the last step, the visualization of glycoproteins is achieved through the reaction product of the bound glycoenzyme. The sensitivity of the glycoprotein detection is most critically dependent on the hydrazide reagent. Thus, dihydrazides were not satisfactory, a trihydrazide was better, and polyhydrazides were the best. Two different polyhydrazides were used. One was based on acrylamide and the other on N-acryloyl-tris(hydroxymethyl)aminomethane. The second one proved to be superior because it gave higher sensitivity with no detectable background staining. We have also investigated the influence of various reaction conditions on staining of glycoproteins having oligomannose and N-acetyllactosamine type glycan chains. Some of them, invertase and fetuin, could be detected with sensitivity similar to that of silver staining in gels and colloidal gold staining on the membranes. The detection of small quantities of Endo H-deglycosylated glycoproteins was possible under standard conditions only if several N-acetylglucosamine residues remained bound to the protein.
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PMID:Polyacrylic polyhydrazides as reagents for detection of glycoproteins. 247 93

The proteins of soybean roots undergoing anaerobiosis can be grouped into three classes. Class 1 proteins are induced severalfold and at least 28 of these were identified by in vivo labeling. These proteins include the enzymes alcohol dehydrogenase (ADH), fructose aldolase, pyruvate decarboxylase, phosphoglucomutase, and lactate dehydrogenase. Class 2 proteins include such enzymes as glucose phosphate isomerase, sucrase, and malate dehydrogenase; their specific activity remains constant in aerobiosis or anaerobiosis. The third class of proteins includes those enzymes such as peroxidase whose activity decreases more than 90% after just 1 day in anaerobiosis. Immunoblotting coupled with two-dimensional chromatography of in vitro translated plant extracts demonstrated that ADH level during anaerobiosis is controlled by its mRNA concentration. Little or no mRNA for ADH was detected in aerobically grown roots. This suggests that the increased level of ADH activity is due to de novo synthesis of the mRNA rather than activation of a sequestered mRNA or superactivation of the protein.
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PMID:Gene regulation during anaerobiosis in soya roots. 262 97

Enzyme immunoassays for 17 alpha-hydroxyprogesterone (17-OHP) were developed. Horseradish peroxidase (HRP), glucose oxidase (GOD), invertase (INV) and glucose-6-phosphate dehydrogenase (G6PDH) were used as label enzymes. Double antibody coated beads or tubes were used for separating the bound and free fractions. Antisera used were prepared by using 4-carboxyethylthio-17-OHP and 3-carboxymethyl oxime-17-OHP-bovine serum albumin as immunogens. The bridge heterologous system was more sensitive than other site heterologous and homologous systems. The minimum amounts of 17-OHP detected were 0.25 and 1.0 pg/tube for fluorescence EIAs using HRP and GOD, and 0.1, 10 and 0.1 pg/tube for chemiluminescence EIAs using GOD, INV and G6PDH, respectively. The reproducibility and correlation with RIA were also studied. The present study demonstrates the feasibility of a neonatal screening for congenital adrenal hyperplasia.
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PMID:Fluorescence and chemiluminescence enzyme immunoassays of 17 alpha-hydroxyprogesterone in dried blood spotted on filter paper. 332 May 34

Antibodies directed against Streptococcus mutans GS-5 intracellular invertase and glucosyltransferase fractions capable of synthesizing primarily water-soluble or insoluble glucans were used to ultrastructurally localize the enzymes by means of the unlabeled antibody peroxidase-antiperoxidase method. This immunocytochemical procedure revealed that the intracellular invertase was associated primarily with the cytoplasmic membrane of the cariogenic organism. The glucosyltransferase complex responsible for insoluble glucan synthesis was localized as aggregates attached to the cell surface or extracellular polysaccharides of strain GS-5. In contrast, the glucosyltransferase activity synthesizing primarily water-soluble glucans was distributed uniformly over the cell surface or in association with extracellular polysaccharides. These results are discussed relative to the sucrose-metabolizing ability of Streptococcus mutans.
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PMID:Localization of Streptococcus mutans GS-5 glucosyltransferases and intracellular invertase. 645 62

Invertase from Baker's yeast (Saccharomyces cerevisiae) and Horseradish peroxidase (HRP) were covalently immobilized on Concanavalin A precoupled to Seralose via carbohydrate moieties. Covalent coupling of glycoenzymes was achieved by periodate induced aldehydic groups of glycosyls with amino groups of Concanavalin A, at different pH values. A bifunctional reagent such as glutaraldehyde crosslinks the glycoenzymes with lectin both intra and intermolecularly. Therefore, attempts were made to introduce covalent linkages between glycoenzymes and Concanavalin A-Seralose without intramolecular crosslinking in either. The immobilized preparations of glycoenzymes exhibited high yield of immobilization and eta value. About 90 and 85% covalent coupling could be observed in invertase and HRP at pH 7.0 respectively, as determined by treatment with 0.5 M methyl alpha-D-mannopyranoside. All immobilized glycoenzyme preparations exhibited marked stabilization towards thermal inactivation.
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PMID:Covalent immobilization of invertase and horseradish peroxidase on concanavalin A-Seralose via carbohydrate moieties. 754 67

Antisera raised against the plant glycoproteins beta-fructosidase and horseradish peroxidase can be fractionated on an affinity column of honeybee venom phospholipase A2 to produce serum fractions that are specific for either the alpha 1-->3 fucose or beta 1-->2 xylose epitopes commonly found on the Asn-linked glycans of plant glycoproteins. This affinity purification strategy relies on the absence of beta 1-->2 xylose from the glycan of the venom protein. Such antibody preparations can be used for the detection of these sugar epitopes on glycoproteins.
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PMID:Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1-->3 fucose or beta 1-->2 xylose. 768 35

Entrapment in human alpha 2-macroglobulin (alpha 2M) of non-proteolytic enzymes was achieved with the help of trypsin covalently attached to Sepharose matrix. While it was also possible to achieve entrapment by the exposure of the alpha 2M: enzyme mixtures to soluble trypsin, use of the immobilized proteinase resulted in improved entrapment yields and also prevented the coentrapment of trypsin. Both soluble and immobilized trypsin transformed alpha 2M to the electrophoretically fast form but the immobilized trypsin required relatively longer incubation to bring about the transformation. Horseradish peroxidase was entrapped in higher yield in alpha 2M compared to the relatively high-molecular-weight invertase. alpha 2M-entrapped peroxidase and invertase appeared highly accessible to their respective substrates, as evident from their relatively unaltered Km values. alpha 2M-associated invertase, in spite of its large dimensions, failed to crossreact with the rabbit anti-invertase antiserum, indicating its physical entrapment rather than any other form of association.
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PMID:Entrapment of nonproteolytic enzymes in alpha 2-macroglobulin using immobilized trypsin. 769 19

Previous studies have suggested that a mannose receptor mediates the phagocytic uptake of effete rod outer segments by retinal pigment epithelial cells. In the present study, the effect of adding a soluble ligand for the mannose receptor, horseradish peroxidase, was examined. Cultured retinal pigment epithelial cells from Long Evans rats were preincubated with various concentrations of horseradish peroxidase for 20 min followed by a challenge of FITC-labeled bovine rod outer segments for 3 h. Both counts of total rod outer segments (bound and ingested) and ingested rod outer segments were determined. Rod outer segment uptake was reduced, in a concentration-dependent fashion, by an average of 60% of control values when horseradish peroxidase was added to retinal pigment epithelial cultures. Similarly, total rod outer segment values were reduced to 50% of controls in the presence of at least a 10 micrograms ml-1 horseradish peroxidase concentration. Horseradish peroxidase inhibition of retinal pigment epithelial phagocytic capacity was reversible. Other high mannose glycoproteins, such as invertase, beta-glucoronidase, and ovalbumin, were equally effective in preventing rod outer segment ingestion by retinal pigment epithelial cells. These data further support the hypothesis that a mannose receptor on the retinal pigment epithelial apical surface facilitates phagocytosis of rod outer segments.
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PMID:Natural, high-mannose glycoproteins inhibit ROS binding and ingestion by RPE cell cultures. 854 90


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