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)

Giant-cell formation induced by macrophage fusion factor (MFF) was not altered after pretreatment of macrophages with trypsin, chymotrypsin, pronase, neuraminidase, phospholipase C, or phospholipase D. Pretreatment of macrophages with either alpha-mannosidase or alpha-glucosidase completely inhibited giant-cell development, without altering macrophage viability. No alteration of giant-cell formation was observed when 0.1 M of L-fucose, N-acetyl-glucosamine, D-arabinose, D-xylose, melibiose, D-glucose, D-galactose, alpha-lactose, sucrose, D-fructose, or maltose was present during incubation of macrophages with MFF. Giant-cell formation was abolished when 0.1 M alpha-D-mannose was present during macrophage incubation with MFF. These results suggest that the protein moiety of MFF recognizes a specific receptor site on the macrophage membrane, one that is different from those described for other lymphokines and contains alpha-mannose.
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PMID:Chemical nature of the interaction between macrophage fusion factor and macrophage membranes. 635 71

Thyroid-stimulating hormone (TSH) subunit glycosylation was compared to that of total cell glycoproteins in mouse thyrotropic tumors. Lipid-linked oligosaccharides, total cell glycoproteins, and TSH subunits were labeled with either [3H]mannose, [3H]galactose, or [3H]glucose in pulse and pulse-chase experiments. The various oligosaccharides were isolated respectively by lipid extraction and mild acid hydrolysis, by selective immunoprecipitation, or by acid precipitation followed by trypsin and endoglycosidase H treatment. The nature of the oligosaccharides was assessed by their migration in paper chromatography, their relative incorporation of different precursors, and also their resistance to alpha-mannosidase. At 60 min, lipid-linked oligosaccharides were found to be composed of Glc3-2Man9GlcNAc2, Man9-8GlcNAc2, and Man5GlcNAc2. At 10 or 60 min of labeling, total cell proteins contained Glc3Man9GlcNAc2, Glc1Man9GlcNAc2, Man9GlcNAc2, Glc1Man8GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2. The largest oligosaccharide, Glc3Man9GlcNAc2, had an unusually long half-life of about 2 h. In contrast, no Glc3Man9GlcNAc2 was found either on TSH + alpha subunits or on free beta subunits isolated either by immunoprecipitation or by sodium dodecyl sulfate gel electrophoresis. Instead, primarily Man9GlcNAc2 was found after a 10-min pulse both on TSH + alpha subunits and on beta subunits. When the pulse was followed by a chase up to 2 h, there was a progressive increase in Man8GlcNAc2 in higher amounts on TSH + alpha-subunit carbohydrate chains than on beta subunits.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Glycosylation and processing of high-mannose oligosaccharides of thyroid-stimulating hormone subunits: comparison to nonsecretory cell glycoproteins. 649 54

Cytotoxic T lymphocytes (CTL) were raised against syngeneic plasmacytoma MOPC-315 cells by culturing spleen cells immunized with MOPC-315 cells 7 to 14 days previously, in the presence of MOPC-315 cells for 5 days. The cytotoxic activity of these CTL was blocked by D-mannose, indicating that mannose-containing carbohydrate moieties are involved in the expression of cytotoxic activity. Investigations were performed to determine which cells, effector or target, possess carbohydrate moieties, by employing procedures by which a part or most of the carbohydrate on cells can be removed. When target cells were treated with 2-deoxy-D-glucose, tunicamycin or trypsin, the levels of cytotoxic activity of the CTL were reduced. However, the reduced activities were still blocked by adding D-mannose at the effector phase. Treatment with alpha-mannosidase did not affect the level of cytotoxicity or mannose-sensitivity. In contrast, when effector cells were treated with tunicamycin by adding it to the culture one day before harvest, the level of cytotoxic activity was reduced, but the cytotoxic activity was no longer blocked by D-mannose. A similar result was obtained when effector cells were treated with periodate after 5 days of culture. However, the treatment of effector cells with alpha-mannosidase did not affect the cytotoxicity of the CTL. Thus, it was shown that effector cells possess mannose-containing carbohydrate moieties which are involved in the full expression of CTL to syngeneic MOPC-315 cells.
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PMID:Involvement of carbohydrate moieties in the expression of effector activity of cytotoxic T cells against syngeneic tumor cells. 660 69

We have investigated the effect of size and location of the oligosaccharide chain on protease degradation of bovine pancreatic ribonuclease. The sensitivity of nonglycosylated RNase A to trypsin and chymotrypsin was compared with three glycosylated species of RNase B which differed with respect to the size of the carbohydrate chain. Two forms of glycosylated RNase B were isolated by concanavalin A-Sepharose affinity chromatography, and each was shown to contain a single carbohydrate chain composed of GlcNAc2Man1 (RNase B") or GlcNAc2Man5-8 (RNase B). A third form (RNase B'), with oligosaccharide composed of GlcNAc2Man4, was prepared by partial digestion of RNase B with alpha-mannosidase. Fully glycosylated RNase B was found to be 6-10 times more resistant to trypsin digestion than nonglycosylated RNase A. RNase B' and B", with intermediate chain sizes, were 3.0- and 1.3-fold more resistant to trypsin digestion than RNase A, respectively. With chymotrypsin, however, differences in rates of digestion were much less marked, with a maximum difference of 3-fold between RNase A and B. In addition, we found that the specificity of the primary trypsin (Arg 33-Asp 34 bond) or chymotrypsin (Tyr 25-Cys 26 bond) cleavage site was not affected by the presence or size of the oligosaccharide chain. These results are consistent with the view that the size of the oligosaccharide chain and its proximity to the primary or rate-limiting cleavage site are important for expression of the carbohydrate protection against proteolytic degradation, which thus appears to be mediated by steric hindrance.
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PMID:Effect of size and location of the oligosaccharide chain on protease degradation of bovine pancreatic ribonuclease. 663 Jan 85

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

The resistance of Candida albicans to amphotericin B methyl ester increases rapidly as cultures enter the stationary phase of growth; organisms harvested after several days in the stationary phase may have a resistance two or three orders of magnitude greater than that of exponentially growing organisms. This resistance is decreased by incubation of the organisms with enzymes which attack components of the cell wall. Of the enzymes tested, (1 leads to 3)-beta-D-glucanases are the most effective; incubation of 7 d batch cultures with exo-(1 leads to 3)-beta-D-glucanase at a concentration of 10 microgram enzyme protein (mg dry wt organisms)-1 for 24 h at 37 degrees C and pH 6.5 reduces the resistance of the organisms to a value approximating to that of exponentially growing organisms. Resistance is also decreased by treatment with chitinase, lipase, trypsin, alpha-mannosidase and (1 leads to 6)-beta-D-glucanases but, on a specific activity basis, none of these enzymes is as effective as (1 leads to 3)-beta-D-glucanase. The action of (1 leads to 3)-beta-D-glucanase is markedly enhanced by the addition during incubation of chitinase, trypsin or lipase.
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PMID:Reduction of amphotericin resistance in stationary phase cultures of Candida albicans by treatment with enzymes. 699 16

When cells of the slime mould Dictyostelium discoideum are allowed to starve in the presence of alpha-chymotrypsin, they are blocked in development at the stage where tight aggregates form tips. Analysis of developmentally regulated enzymes has shown that alpha-mannosidase, beta-N-acetylglucosaminidase, threonine deaminase, tyrosine aminotransferase, beta-glucosidase and the carbohydrate-binding protein discoidin are unaffected, but enzymes that show an increase in specific activity during post-aggregative development, namely glycogen phosphorylase, UDP-glucose pyrophosphorylase, UDP-galactose 4-epimerase, UDP-galactose polysaccharide transferase and alkaline phosphatase, did not show the characteristic increase when development was blocked by alpha-chymotrypsin. Recovery of cells from the effects of alpha-chymotrypsin was accompanied by the formation of fruiting bodies and a concomitant increase in the specific activity of UDP-glucose pyrophosphorylase. Uptake or efflux of 45Ca2+ was not altered in the presence of alpha-chymotrypsin. Cells allowed to develop in alpha-chymotrypsin, or treated with the enzyme for 15 min, had a markedly reduced ability to bind cyclic AMP with low affinity; high-affinity binding was unaffected. Pronase had a similar effect on cyclic AMP binding, but trypsin, which does not alter developmental processes, has no effect on cyclic AMP binding to D. discoideum cells.
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PMID:Developmentally regulated enzymes and cyclic AMP-binding sites in Dictyostelium discoideum cells blocked during development by alpha-chymotrypsin. 715 Feb 39

Membrane fractions have been isolated from eggs of Fucus serrratus which inhibit fertilization in a species-specific manner. This activity is destroyed by alpha-fucosidase and alpha-mannosidase. Some 6% of the protein of this membrane fraction binds to Con A-agarose, following SDS solubilization, and when eluted with alpha-methyl mannoside inhibits fertilization when preincubated with sperm, but not eggs. This inhibitory activity is species-specific and destroyed by alpha-fucosidase but not by trypsin. SDS-gel electrophoresis reveals 1 band staining strongly with Coomassie Brilliant Blue G and weakly with the PAS reagent. This major band represents a glycoprotein with an approximate molecular weight of 30 000 Daltons. Membrane fractions from sperm of Fucus serratus solubilized in KC1 yielded a protein-containing fraction, after affinity chromatography on desulphated focoidan-Sepharose. This fraction is 100-fold more effective in inhibiting fertilization after preincubation with eggs than either Con A or fucose-binding protein. It is species-specific and inhibition is reversed when pretreated eggs are washed with fucoidan. Activity is destroyed by heat and trypsin and only one diffuse band is apparent on SDS gels. This stains positively with Coomassie Brilliant Blue G but not with PAS and has a molecular weight of approximately 60 000 Daltons. Tentative calculation of the numbers of putative receptor molecules gives a figure of 2.5 X 10(9) receptors per egg and 1.8 X 10(6) receptors per sperm.
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PMID:Fertilization in brown algae. III. Preliminary characterization of putative gamete receptors from eggs and sperm of Fucus serratus. 719 29

Culture supernatant, prepared by incubating fetal calf serum and liposome-treated B cells, augments mouse peritoneal macrophage Fc gamma receptor-mediated phagocytosis of IgG-opsonized sheep red blood cells. The activation process was hypothesized to be as follows. B-cell membranous glycosidases stimulated by liposomes, convert serum factor to a macrophage-stimulating active serum factor. As the active serum factor loses its activation potential by the addition of mannose or by digestion with alpha-mannosidase, mannose residues at the terminal present in the active serum factor are hypothesized to contribute to macrophage activation. The active serum factor was purified on a concanavalin A-Sepharose 4B column, and identified as a modified form of alpha 2-macroglobulin by immunochemical analysises. On non-denaturing polyacrylamide gel electrophoresis, modified alpha 2-macroglobulin showed a slow form, while alpha 2-macroglobulin-trypsin and alpha 2-macroglobulin-methylamine complexes, which bind specifically to alpha 2-macroglobulin receptors, showed a fast form and did not activate macropahges. These findings demonstrate that alpha 2-macroglobulin is the essential serum factor in liposome-primed macrophage activation, and that modified alpha 2-macroglobulin with mannose residues at the terminal sugar chain binds to macrophage mannose receptors, but not alpha 2-macroglobulin receptors, and increases Fc gamma receptor-mediated phagocytosis of IgG-opsonized sheep red blood cells.
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PMID:Identification of the serum factor required for liposome-primed activation of mouse peritoneal macrophages. Modified alpha 2-macroglobulin enhances Fc gamma receptor-mediated phagocytosis of opsonized sheep red blood cells. 759 Aug 84

Three different carbohydrate-depleted enzymes were prepared from an endo-beta-1,4-glucanase of Aspergillus niger IFO31125 by treatment with endo-beta-N-acetylglucosaminidase or alpha-mannosidase. They were purified by Concanavalin A-Sepharose affinity and DEAE ion-exchange column chromatographies. The molecular sizes of these enzymes had been decreased from 40 kDa containing 9.0% carbohydrate to 39, 38, and 37 kDa with carbohydrate at 4.5, 1.3, and 0.8% (wt/wt), respectively. The native and these carbohydrate-depleted enzymes were compared in their enzymatic properties, and it was found that they were identical in their catalytic activities and both thermal and pH stabilities. However, the 37-kDa enzyme was more susceptible to proteolysis by Savinase, proteinase K, and Pronase E. On the other hand, the specific protease trypsin showed no such effect on activity of all enzymes. These results suggested that the core structure of the asparagine-linked sugar chain, which consisted of three monosaccharide residues, contributed to the high stability of the endo-beta-1,4-glucanase against protease digestion.
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PMID:Effects of size of carbohydrate chain on protease digestion of Aspergillus niger endo-beta-1,4-glucanase. 761 90


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