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:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Egg lectin of Rana japonica, which specifically agglutinates transformed cells but does not agglutinate nontransformed cells and erythrocytes, has been isolated by gel filtration and successive ion-exchange chromatographies on diethylaminoethyl cellulose and carboxymethylcellulose columns and has been characterized as a homogeneous carbohydrate-free protein with a relative molecular weight of 13,500. The lectin, at a concentration of 1 microgram/0.1 ml, causes obvious cytoagglutination of various transformed and tumor cell. The receptor of the Erlich ascites tumor cells which inhibits the lectin-induced agglutination of the Ehrlich ascites tumor cells has been isolated and characterized. The receptor was solubilized from Ehrlich ascites carcinoma cells by treating a tumor cell suspension with insolubilized trypsin, and the solubilized receptor was isolated by gel filtration through Sephadex G-100, followed by ion-exchange chromatography on diethylaminoethyl cellulose. The receptor was identified as a homogeneous glycoprotein having about 25% carbohydrate. The receptor, at a concentration of 4 microgram/0.1 ml, completely inhibited the cytoagglutination of the Ehrlich carcinoma cells caused by three agglutination doses (about 3 microgram/0.1 ml) of the R. japonica lectin.
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PMID:Egg lectin of Rana japonica and its receptor glycoprotein of Ehrlich tumor cells. 57 Apr 54

Ten-day-old embryonic chick neural retina release into the environment glycoprotein ligands which bind to homologous cells, inhibiting the lectin-induced redistribution of cell surface receptors. Material with identical activity is released from trypsin-dissociated neural retina cells that are allowed to repair in culture for 2 h and are then transferred to fresh medium. Release of ligand is inhibited by cytosine arabinoside, hydroxyurea, UDP, and EDTA, and is potentiated by MnCl2. These data suggest that a glycosyltransferase reaction plays a critical role in the turnover of the cell surface ligand. Reactivation of enzymatically deglycosylated ligand solutions by intact cells provides further support for this hypothesis. Release of ligand is also accompanied by a loss of the agglutinability of the cells by a tissue-specific component which accumulates in monolayer conditioned medium. Conditions which inhibit release maintain maximal agglutinability suggesting similar mechanisms mediate both processes.
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PMID:The turnover of a tissue specific cell surface ligand which inhibits lectin induced capping. 61 88

Capacitated guinea pig sperm are more agglutinable by the lectin soybean agglutinin (SBA) than uncapacitated sperm (Talbot and Franklin, '78). This study demonstrates that uncapacitated guinea pig sperm become as agglutinable by SBA as capacitated sperm when treated with trypsin, but not chymotrypsin. The pattern of lectin induced sperm agglutination after trypsinization resembles that for capacitated sperm. Also, trypsinization specifically increases SBA induced agglutination and does not affect agglutination by RCA-60; similar results are obtained during in vitro capacitation. Taken together, these data may indicate that a trypsin-like enzyme modifies the sperm surface during capacitation.
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PMID:Trypsinization increases lectin-induced agglutinability of uncapacitated guinea pig sperm. 64 90

The effects of concanavalin A (Con A) and leucoagglutinin (LA) on the locomotor response of phagocytes have been studied in vitro. At concentrations of 1 to 4 microgram/mol, Con A and LA induced maximal chemokinesis and chemotaxis of monocytes, macrophages and, to a lesser degree, also of neutrophils. The lectin-induced locomotion was accompanied by membrane alterations and metabolic changes, as shown by an increase of the 3H-uridine uptake and a rise of the hexose monophosphate shunt activity. The chemotactic activity of Con A was inhibited by alpha-methyl mannoside (50 mM) or by pretreatment of the cells with trypsin. These data indicate that lectins such as Con A induce chemotaxis by a specific binding to receptors of the cell membrane. It is suggested that bivalent ligand binding is required as a signal to elicit chemotactic locomotion.
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PMID:Chemotactic activity of lectins in vitro. 64 77

Living, intact bloodstream trypomastigotes and culture procyclic forms of Trypanosoma congolense were tested for aggulination with the lectins concanavalin A (Con A), phytohemagglutinin P (PP), wheat germ agglutinin (WGA), soybean agglutinin (SBA), and fucose binding protein (FBP). Similar experiments were conducted with living bloodstream and culture forms treated with trypsin or dextranase. Parasites were incubated for 30 min at 25 C in various concentrations of each lectin, then examined for agglutination by dark-field microscopy. Control preparations consisted of parasites incubated alone or with 0.5 M of the specific competing sugar, with or without the corresponding lectin. Electron-microscopic localization of lectin binding sites on the surface of intact and dextranase-treated bloodstream and intact culture forms was accomplished with Con A, reacted with horseradish peroxidase (HRP) and then diaminobenzidine (DAB). In addition, FBP and SBA were coupled to HRP, then utilized for the localization of binding saccharides on the surface of bloodstream forms by the DAB technic. Similar studies were conducted with culture procyclics incubated with WGA-, SBA-, PP- or FBP-HRP conjugates and then reacted with DAB. Controls were utilized to confirm the sugar specificity of all positive reactions. Intact living bloodstream forms were agglutinated in a concentration-dependent manner with all the lectins tested. Agglutination levels were scored as Con A greater than FBP greater than WGA = PP = SBA. Sugars resembling alpha-D-mannose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, and alpha-L-fucose are evidently present on the surface of the parasites. No agglutination was noted in any control preparations. Identical lectin-induced agglutinations were obtained with trypsin- or dextranase-treated bloodstream forms. Trypsin disrupted but did not entirely remove the surface coat of bloodstream forms, while dextranase did not alter the ultrastructure of the parasites. Con A-, SBA- and FBP-binding saccharides were distributed uniformly on the surface coat of intact bloodstream forms; a similar distribution of Con A receptors was noted also on the surface of dextranase-treated cells. No lectin-binding saccharides were visualized by electron microscopy on any control preparations. Intact, trypsin- or dextranase-treated, procyclics were agglutinated in a concentration-dependent fashion by Con A and WGA, but not by the other lectins tested. Control preparations did not agglutinate and the enzymes did not affect the ultrastructure of the parasites. Con A- and WGA-specifically binding saccharides were uniformly distributed on intact procyclics and control preparations were lectin-negative. Thus, T. congolense procyclics retained surface saccharides resembling alpha-D-mannose and N-acetyl-D-glucosamine but lost sugars resembling N-acetyl-D-galactosamine (or D-galactose) and alpha-L-fucose...
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PMID:Lectin analysis of Trypanosoma congolense bloodstream trypomastigote and culture procyclic surface saccharides by agglutination and electron microscopic technics. 73 11

Purified and desialylated glycoprotein M from human O erythrocytes precipitates with B and H specific lectin from Evonymous europaeus seeds, both in PBS and 0.2% Triton X-100. Desialylated, N-terminal fragment (MT-1) obtained by trypsin digestion of M glycoprotein does not precipitate with Evonymous lectin but inhibits precipitation.
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PMID:Localization and immunochemical characterization of the lectin Evonymous europaeus receptor site on the glycoprotein from human O erythrocytes. 74 64

The lectin present in the mucus of the snail Arion empiricorum was isolated by ion exchange chromatography. Purity was demonstrated by immunelectrophoretic analysis, immunization studies, and polyacrylamide gel electrophoresis. With the latter we found a molecular weight of 43,000. Hemagglutination inhibition studies revealed that carbohydrates play a minor role in the agglutination reaction of A. empiricorum lectin. Stronger inhibition could be achieved with human serum and the serum of several animal species. These findings were clarified by the demonstration that some serum proteins were precipitated by A. empiricorum lectin. Besides its agglutinating and precipitating properties the purified A. empiricorum lectin possesses proteinase-inhibiting properties, as demonstrated by the inhibition of casein-digestion by trypsin and plasmin.
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PMID:Isolation and new biological properties of Arion empiricorum lectin. 76 Aug 14

The lectin content of some native plants in Taiwan was studied. The majority of the plants possessing lectin belonged to Leguminosae. Five lectins which are readily available were further studied for their hemagglutination titers, specificity, susceptibility to heat and proteolytic enzymes. The lectins of Ricinus communis had hemagglutination titer of 1:512 which was the highest among the five tested. All lectins were heat labile, destroyed by heating at 100 degrees C for 30 min, but resistant to trypsin and pepsin. The resistance was not due to the presence of any inhibitor in the crude extract, but possibly due to the special configuration of the lectin molecule or other unknow reasons. Among the five lectins only the lectin of Phaseolus vulgaris could not be inhibited by any of the carbohydrates tested. It seems that the lectin of Phaseolus vulgaris is nonspecific, or not specific for ABO blood group, or specific for other blood groups. The inhibiting activity of carbohydrates seems to be specific. The configuration of carbohydrates at carbon atom 2 and/or 4, the type of linkage (alpha or beta), or the carbon number where the linkage is formed seem to be important to the potency of carbohydrates to inhibit the activity of lectin.
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PMID:Studies of native plants in Taiwan for lectin content. 77 95

The cell-to-cell binding induced by concanavalin A (Con A) and the lectins from wheatgerm, soybean, and waxbean has been analyzed by measuring the ability of single cells to bind to lectin-coated cells immobilized on nylon fibers. The cells used were lymphoma, myeloid leukemia, and normal fibroblast cells. With all lectins, cell-to-cell binding was inhibited if both cells were prefixed with glutaraldehyde. However, in most cases cell-to-cell binding was enhanced when only the lectin-coated cell was prefixed. With normal fibroblasts, treatment of either one or both cells with trypsin enhanced the cell-to-cell binding induced by Con A and the wheatgerm lectin. Neuraminidase, which increases the number of receptors for soybean agglutinin, increased cell-to-cell binding only if both cells were treated. Although cell-to-cell binding induced by the lectins from soybean and wheatgerm could be partially reversed by the appropriate competitive saccharide inhibitor, binding induced by Con A could not be reversed. The experiments indicate that cell-to-cell binding induced by a lectin can be prevented by an insufficient density of receptors for the lectin, insufficient receptor mobility, or induced clustering of receptors. These effects can explain the differences in cell-to-cell binding and agglutination observed with different cell types and lectins. They also suggest that cell-to-cell binding induced by different lectins with a variety of cell types is initiated by a mechanism involving the alignment of complementary receptors on the colliding cells for the formation of multiple cell-to-lectin-to-cell bridges.
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PMID:Cell-to-cell binding induced by different lectins. 80 50

A soluble lectin which agglutinates trypsin-treated rabbit erythrocytes was purified from calf heart using affinity chromatography on asialofetuin-Sepharose. Its molecular weight was determined by gel filtration to be approximately 17,000. On polyacrylamide gel electrophoresis in sodium dodecyl sulfate, the predominant molecular species had a molecular weight of 9,000, suggesting that the lectin is a dimer. Binding studies performed with iodinated lectin revealed that neuraminidase-treated calf erythrocytes contained approximately 5 X 10(6) lectin binding sites per cell. Native calf and rabbit erythrocytes bound the lectin, but human and rat erythrocytes required neuraminidase and trypsin treatment, respectively, for lectin binding to occur. A number of saccharides, glycopeptides, and glycoproteins possess haptene inhibitory activity toward lectin binding to erythrocytes. The most potent of these have either galactose beta leads to galactose beta leads to, galactose beta N-acetylglucosamine beta leads to, or galactose beta leads to N-acetylglucosamine beta leads to sequences at their nonreducing termini. Lactose and galactose beta 1 leads to 3N-acetylgalactosamine are the next best haptenes. Finally, alpha-linked galactose residues and free galactose are very weak haptenes. The presences of a terminal sialic acid residue impairs haptene activity in all instances. Calf heart also contains a membrane-associated lectin which is very similar but not identical with the soluble lectin. A soluble beta-galactoside binding lectin was also isolated from calf lung. It has the same molecular size and subunit structure as the soluble heart lectin and is antigenically identical. In binding studies, the pattern of inhibition by various haptenes was the same for all three lectins.
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PMID:Isolation and properties of beta-galactoside binding lectins of calf heart and lung. 82 31


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