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)

In an effort to assess the impact of enhanced macrophage function in acute pancreatitis, mice were subjected to a choline-deficient diet supplemented by ethionine to induce necrotizing pancreatitis. Treatment with the macrophage stimulant glucan resulted in improved survival rates (58 percent versus 14 percent) and maintenance of pancreatic architecture. Glucan treatment also resulted in decreased plasma and peritoneal trypsin activity, as well as increased trypsin-binding activity in the blood and peritoneal cavity. Plasma interleukin-1, as well as macrophage production of interleukin-1, were increased in the glucan-treated mice, which indicated enhanced macrophage function. These composite findings suggest that by enhancing diverse aspects of reticuloendothelial function, clinical use of immunomodulators may have significant impact on the pathogenesis of acute pancreatitis.
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PMID:Protective effect of glucan-enhanced macrophage function in experimental pancreatitis. 379 90

Membrane preparations from the non-photosynthetic alga Prototheca zopfii incorporate glucose from UDP-[3H]glucose into the trichloroacetic-acid-insoluble fraction and the polysaccharides insoluble in hot alkali. Time course and pulse-chase experiments indicate that the acid-insoluble fraction was a precursor of the alkali-insoluble fraction. Isolation of 3H-labeled membrane or soluble fraction showed that only membrane fractions were able to transfer radioactivity into polysaccharides. Treatment of glucosylated membranes with trypsin or cellulase only partially affect their transfer ability, indicating that the precursor was internalized in vesicles. Analysis of the in vitro synthesized polysaccharides by enzymatic and acid hydrolysis showed that glucose and cellobiose were present as radioactive sugars. Permethylation of the polysaccharide indicates that 80% of the glucose was beta-1,4-bonded with 20% in beta-1,3-linkages. This polysaccharide was found to be identical with the cell-wall beta-glucan obtained in vivo [Rivas, L.A. & Pont Lezica, R. (1978) Planta (Berl.) 165, 348-353].
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PMID:Synthesis of beta-glucans in Prototheca zopfii. Evidence for the existence of a glycoprotein primer. 381 92

Cell walls isolated from two strains of Blastomyces dermatitidis were examined. Whereas strain Ga-1 was practically avirulent for mice, strain KL-1 produced death by 21 days in 50% of the mice inoculated. Analyses of the trypsin-treated cell walls of the two strains revealed a higher chitin and protein content in strain KL-1, whereas a higher polysaccharide content was observed in the cell walls of strain Ga-1. Extraction of the walls with 1 n NaOH revealed a threefold difference in the amount of alkali-soluble cell wall material present. The alkali-soluble material could be further fractionated into a water-soluble and a water-insoluble fraction. Previous reports have indicated that the water-insoluble fraction of B. dermatitidis consists of an alpha-linked glucan; however, we report that in addition a phospholipid moiety is covalently bound to the polysaccharide. Furthermore, on the basis of organic phosphorus content, considerably more phospholipid is associated with the alpha-linked glucan of the more virulent KL-1 strain. These results suggest that this cell wall constituent might be one of the factors related to the virulence of this fungus.
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PMID:Cell wall composition of two strains of Blastomyces dermatitidis exhibiting differences in virulence for mice. 463 84

In the pigeon, 70-80% of the activities of maltase (alpha-D-glucoside glucohydrolase EC 3.2.1.20), sucrase (alpha-glucohydrolase, EC 3.2.1.48), isomaltase (dextran 6-alpha-D-glucan hydrolase, EC 3.2.1.10) and glucoamylase (1,4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) were found to be localized in the brush-border membrane of intestinal epithelial cells. Of the total glycosidase activities in the mucosal homogenate, nearly 60 to 70% were recovered in the microsomal (105 000 X g) fraction, about 30% in the mitochondrial (22 000 X g) fraction and less than 5% from the cytosol (105 000 X g supernatant) fraction. The hydrolases were solubilized by digestion with papain but not with trypsin, and the phosphate ion had a protective effect in the solubilization. Amongst detergents, Triton X-100 but not sodium deoxycholate, was found to truly solubilize these enzymes.
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PMID:Studies on the intestinal disaccharidases of the pigeon. II. Subcellular localization and solubilization. 618 28

1.4-alpha-glucan branching enzyme (EC 2.4.1.18) from rabbit muscles with an essential 2.5S RNA component has been studied by limited trypsin treatment. Under a great variety of hydrolysis conditions the product resistant to subsequent action of trypsin was obtained. This product contains about 70% of protein and all 2.5S RNA of the original nucleoprotein and retains about 50% of original activity. Amino acids Composition showed, that the protein is of alkaline nature and is rich in lysine. The alkaline nature of protein remains unchanged after trypsinolysis. On the basis of these studies it was assumed that the presence of firmly attached to the protein 2.5S RNA protects the branching enzyme against more powerful trypsinolysis and hinders loss of activity of the branching enzyme.
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PMID:[Structure-function study of 1,4-alpha-glucan branching enzyme by limited trypsin treatment]. 621 6

The appearance and continuing growth of extracellular material on Streptococcus mutans HS6 cells in sucrose-containing Merthiolated buffer was observed in a scanning electron microscope and was found to be related to the glucan synthesis on the cell and to adherence of the cell to a smooth surface. Cells grown in broth completely deprived of sucrose by invertase (HS6-IV) had a characteristic, slightly rugged surface structure. On incubation of HS6-IV in the sucrose-containing buffer, a few small globular particles appeared on the surface and grew to an irregular shape (globular to fibrilar) after several hours. The increase in the total glucan content of the cells paralleled the growth of the globular material, to which ferritin-conjugated anti-dextran globulin was found to bind. On the cell surface of cells harvested from conventional broth, both small globular and irregular structures, which possibly formed from sucrose in the broth, existed originally and continued to grow during incubation, along with the material newly appearing on the surface. The accumulation of glucan on the cells resulted in their adherence to a glass surface. The inhibition of growth of the extracellular material on the cells by trypsin, dextranase or anti-glucosyltransferase corresponded to the decrease in glucan synthesis and the loss of adhering ability. These results indicated that the material growing on the cell surface was glucan synthesized by glucosyltransferases.
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PMID:Synthesis of glucan on the cell surface of Streptococcus mutans: chemical and scanning electron microscopic studies. 621 5

Yeast lytic activity was purified from the culture supernatant of Oerskovia xanthineolytica grown on minimal medium with insoluble yeast glucan as the carbon source. The lytic activity was found to consist of two synergistic enzyme activities which copurified on carboxymethyl cellulose and Sephadex G-150, but were resolved on Bio-Gel P-150. The first component was a beta-1,3-glucanase with a molecular weight of 55,000. The K(m) for yeast glucan was 0.4 mg/ml; that for laminarin was 5.9 mg/ml. Hydrolysis of beta-1,3-glucans was endolytic, yielding a mixture of products ranging from glucose to oligomers of 10 or more. The size distribution of products was pH dependent, smaller oligomers predominating at the lower pH. The glucanase was unable to lyse yeast cells without 2-mercaptoethanol or the second lytic component, an alkaline protease. Neither of these agents had any effect on the glucanase activity on polysaccharide substrates. The protease had a molecular weight of 30,000 and hydrolyzed Azocoll and a variety of denatured proteins. The enzyme was unusual in that it had an affinity for Sephadex. Although the activity was insensitive to most protease inhibitors, it was affected by polysaccharides; yeast mannan was a potent inhibitor. The enzyme did not have any mannanase activity, however. Neither pronase nor trypsin could substitute for this protease in promoting yeast cell lysis. A partially purified fraction of the enzymes, easily obtained with a single purification step, had a high lytic specific activity and was superior to commercial preparations in regard to nuclease, protease, and chitinase contamination. Lyticase has been applied in spheroplast, membrane, and nucleic acid isolation, and has proved useful in yeast transformation procedures.
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PMID:Lyticase: endoglucanase and protease activities that act together in yeast cell lysis. 699 73

Mutants of Candida utilis and a haploid strain of Saccharomyces cerevisiae were isolated, after ultraviolet light mutagenesis, which had increased sensitivities to snail gut enzymes (ses). Three of the five S. cerevisiae mutants tested had increased sensitivities to porcine pepsin, all were more susceptible to a sequential treatment with pepsin, lipase, peptidase, and trypsin, four were sensitive to osmotic shock, and two had increased glucan/mannan ratios in their cell walls. All combinations of mutants showed positive complementation in heterozygous diploids, although complementation between one pair, which had the same phenotype, was incomplete, indicating that four to five different cistrons were involved. All mutations were found to be recessive. Haploid strains bearing pairs of ses mutations were not markedly more sensitive to mammalian digestive enzymes than strains with single mutations. Rat-feeding experiments with three mutants and the parental strains indicated that the protein was efficiently utilized in all cases. Net protein ratios for the two mutants of S. cerevisiae tested were slightly higher than that for their parent, but the differences were of marginal significance.
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PMID:Mutants of Saccharomyces cerevisiae and Candida utilis with increased susceptibility to digestive enzymes. 701 34

The objectives of this study were to determine whether intestinal viscosity caused by mixed linked barley beta-glucan depresses ileal nutrient digestibility and digestive enzyme activities and to determine the interaction of intestinal viscosity, digestive enzyme activities and ileal nutrient digestibility in different ages of poultry. In Experiments 1 and 2, 1-d-old broiler chicks and 1-y-old cocks, respectively, were fed diets with 60% corn, low and high viscosity barley with or without beta-glucanase, for 3 wk. A 3 x 2 factorial design was used. Comparisons were made only within the same age group. In Experiment 3, 1-d-old broiler chicks were fed high viscosity barley with and without beta-glucanase to measure fecal nutrient and ileal and fecal amino acid digestibility. Broiler chicks fed barley ate less and gained less weight than those fed corn; added beta-glucanase resulted in increases in both food consumption and weight gain for the barley-fed chicks (P < 0.05). Relative pancreas weight was higher (P < 0.05) in chicks fed barley than in those fed corn, and lower with beta-glucanase (P < 0.05). Digesta from barley-fed birds had the highest viscosities, which were decreased (P < 0.05) by beta-glucanase. Amylase and lipase were lower in broiler chicks fed high viscosity barley compared with corn (P < 0.05), and beta-glucanase increased both activities and that of trypsin as well (P < 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The differences in intestinal viscosity produced by barley and beta-glucanase alter digesta enzyme activities and ileal nutrient digestibilities more in broiler chicks than in cocks. 753 29

A receptor for beta-glucan was in the present study shown to mediate binding of zymosan particles to resident mouse peritoneal macrophages. Lysosomal enzyme secretion in response to zymosan was maximal at a low particle/cell ratio, continuous for at least 3 h after particle/cell contact and inhibitable by soluble glucan. Latex particles of various size caused no selective secretory response, but at high particle/cell ratios were toxic. By use of a fluorescent ligand, the macrophage beta-glucan receptor was shown to be trypsin-sensitive, Ca2+/Mg(2+)-independent, recirculating and also present in an intracellular mobilizable pool. Binding of ligand to the beta-glucan receptor and inhibition of the lysosomal secretory response to zymosan were both more efficient with glucans of larger size, indicating that clustering of glucan receptors at the cell surface occurs. Such clustering could stabilize ligand binding by multiple interactions and possibly trigger intracellular signaling events on binding of zymosan particles.
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PMID:Glucan receptor and zymosan-induced lysosomal enzyme secretion in macrophages. 770 80


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