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:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Blood enzymatic activities in gastric carcinoma depend on the release from carcinomatous tissues, surrounding non-neoplastic tissues, increased permeability and necrosis of carcinomatous tissues. However, those enzymatic activities did not parallel the extent and macroscopic appearance of the tumor. Various enzyme proteins and gastrointestinal hormones concerning gastric carcinoma and intestinal metaplasia including pepsin, LDH, AFP, beta-glucuronidase, rGTP, lysozyme, ferritin, sialic acid, polyamine, CEA, Ca 19-9, collage, gastrin, immunoglobulin are discussed in this paper. The variation of enzymes and proteins occurring in gastric carcinoma and intestinal metaplasia are well documented. Some of them would be a useful indicator of diagnosis and treatment as a tumor marker.
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PMID:[Various enzymatic activities in gastric carcinoma and intestinal metaplasia]. 309 81

Monkey pepsinogen A, monkey progastricsin, and porcine pepsinogen A were activated in the presence of two different protein substrates, namely, reduced and carboxymethylated lysozyme and hemoglobin. In each case, an extensive delay in activation was observed. The intermolecular activation reaction required for the generation of pepsin or gastricsin was strongly inhibited and this inhibition was essentially responsible for the delay. However, the intramolecular reaction required for the generation of the intermediate forms of the proenzymes was scarcely affected. The delay was longer at pH 3.0 than at pH 2.0. Irrespective of the delay in activation of pepsinogen, the digestion of substrates proceeded rapidly, evidence of the significant proteolytic activity of pepsinogen itself. Kinetic experiments demonstrated that pepsinogen changed from an enzymatically inactive species to an active species before the release of the activation segment. The proteolytic activity of the active pepsinogen was highest at pH 2.0, at 37 degrees C and the activity under these conditions was comparable to that of pepsin.
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PMID:Analysis of the activation of pepsinogen in the presence of protein substrates and estimation of the intrinsic proteolytic activity of pepsinogen. 313 9

Tryptophan pyrrolooxygenase from wheat germ was separated into three molecular forms by microgranular DEAE-cellulose using a stepwise or a linear gradient elution procedure. In the first case molecular forms A and B were eluted with 10 mM Tris/HCl buffer (pH 7.4) and molecular form C was eluted with 50 mM KCl in the same buffer. The same separation could also be achieved with a linear KCl gradient (0-100 mM) in 10 mM Tris/HCl buffer (pH 7.4). The three molecular forms of tryptophan pyrrolooxygenase oxidized L-, D-, DL-Trp as well as many Trp derivatives with formation of N-formylkynurenyl derivatives. They also efficiently oxidized Trp-Phe, Trp-Tyr, Trp-Ala, Ala-Trp, Trp-Gly, Gly-Trp, Trp-Leu, Leu-Trp, Pro-Trp and Val-Trp, although the dipeptides were oxidized at different rates by the three molecular forms. A number of tryptophyl-containing tetra-, penta-, octa-, nona- and decapeptides were also oxidized. The oligopeptides which were known to have a helical conformation were better substrates than the smaller oligopeptides which were devoid of the conformational factor. The three molecular forms of tryptophan pyrrolooxygenase oxidized the tryptophyl residues of lysozyme, pepsin, chymotrypsin, trypsin and bovine serum albumin. It was found that molecular form A oxidized the more exposed (or hydrophilic) Trp residues of the proteins, while molecular form C also oxidized the Trp residues of a more hydrophobic nature. The three molecular forms were inhibited by chelating agents (alpha, alpha'-dipyridyl, EDTA and omicron-phenanthroline), although they differed in their sensitivities to these agents. Their optimum temperatures and inactivation rates at 65 degrees C was also different.
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PMID:Separation of tryptophan pyrrolooxygenase into three molecular forms. A study of their substrate specificities using tryptophyl-containing peptides and proteins. 369 18

Phenol has been added to the Coomassie Brilliant Blue G-250 dye reagent used in the standard Bradford protein assay and its effect upon the reagent blank and assay response of fourteen proteins investigated. Phenol can enhance or impair colour yield depending upon its concentration and the amount and type of protein assayed. Four characteristic protein responses to increasing assay concentrations of phenol have been observed. These indicate a complex influence of phenol upon the protein assay. Dye reagent containing 0.5% phenol gave optimal colour yield with most of the proteins investigated and an improved assay response of ovalbumin, ribonuclease, lysozyme, insulin, pepsin and chymotrypsinogen-A relative to bovine albumin.
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PMID:Phenol addition to the Bradford dye binding assay improves sensitivity and gives a characteristic response with different proteins. 378 18

Immunohistochemical staining of tuberculoid and lepromatous leprosy skin lesions was performed using various rabbit antisera. Macrophages in both stained with serum containing antibodies against lysozyme and alpha-1-antitrypsin, while macrophages in lepromatous leprosy also reacted with other antibodies. An immunoglobulin fraction of positive serum stained following pepsin digestion, indicating that reactivity was not Fc dependent. Positive serum contained antibody against Mycobacterium butyricum, which caused macrophage staining, since affinity-purified antibody did not stain and absorption with M. butyricum removed staining. Staining was also produced by serum of subjects with leprosy or a positive tuberculin test. By immunoblotting, the anti-mycobacterial antibody was directed against surface components of M. butyricum of molecular weights 20 000-70 000. Electron microscopy showed M. leprae in phagolysosomes of macrophages, while immunoelectron microscopy demonstrated labelling along bacterial cell membranes. Therefore, macrophages in lepromatous leprosy skin lesions stain because they contain M. leprae, which reacts with antibody to either M. leprae, M. tuberculosis or atypical mycobacteria in human serum and with antibody to M. butyricum in serum from rabbits immunized with various antigens and Freund's complete adjuvant. These results indicate that immunohistochemical studies on leprosy are misleading if performed using intact polyclonal immune sera rather than affinity purified or monoclonal antibodies.
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PMID:Immunohistochemical staining of macrophages in the skin lesions of leprosy: the role of antibody to mycobacteria in human serum and various polyclonal immune rabbit antisera. 390 21

An antigen of Streptococcus mutans has been extracted from HS6 (group "a") whole cells and repeatedly fractionated by Sephadex chromatography. The antigen is shown to be a polysaccharide and contains the S. mutans group "a" antigenic site and also a second antigenic site which is common to "a" strains and 2 of 3 group "d" strains. Immunological electrophoretic and chromatographic data indicate that the two sites exist in a single molecule. The polysaccharide has a molecular weight of 107,000 and is composed of glucose, galactose, glucosamine, and galactosamine. No significant quantities of lipid, phosphorus, glycerol, or ribitol are present. Immunological specificity of the group "a" polysaccharide site depends primarily on a d-glucose . d-glucose sequence, the "a-d" site on a terminal d-galactose. Water at 100 C and pepsin (pH 2.5) at room temperature are very effective in extracting the polysaccharide from lyophilized S. mutans cells. Trypsin and lysozyme are less effective. The antigen-antibody combining site appears to be located at the cell wall surface. A small quantity of enzyme-resistant protein (5%) is firmly linked to the antigen and is considered to be a remnant of a protein to which the polysaccharide is attached in the cell wall. The composition of the protein does not identify it as a part of the peptidoglycan. No reaction to the purified polysaccharide is obtained with antisera specific for teichoic acid glycerophosphate polymers from streptococci, staphylococci, or lactobacilli.
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PMID:Extraction, purification, and chemical and immunological properties of the Streptococcus mutans group "a" polysaccharide cell wall antigen. 419 54

Satisfactory Raman spectra of crystalline lysozyme, pepsin, and alpha chymotrypsin were obtained with laser excitation. The spectra are very similar to each other, but show enough minor differences to make this a useful method of identification. The readily identified bands assignable to specific groupings are noted.
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PMID:Raman spectra of crystalline lysozyme, pepsin, and alpha chymotrypsin. 487 94

Resting spores of Bacillus megaterium ATCC 9885 were found to be markedly affected by lysozyme. Exposure to as little as 1.5 mug of lysozyme per ml caused the spores to lose refractility, the darkened spores to shed their coat structures, and the spore central bodies to lyse. The spores of seven other strains of B. megaterium and seven other Bacillus species were not similarly affected by lysozyme. Proteolytic enzymes such as pronase, trypsin, pepsin, and subtilisin did not induce the change. The action of lysozyme differed in certain important respects from that of common "physiological" germinants. Its action was considered to be direct via its enzymatic attack on exposed sites directly accessible in the resting spores of B. megaterium ATCC 9885.
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PMID:Effect of lysozyme on resting spores of Bacillus megaterium. 497 88

The biological activity of Odontomyces viscosus, which has been reported to cause periodontal disease in hamsters, was examined. The microorganism was cultured anaerobically in Brain Heart Infusion broth, and the cells were harvested. The washed cells were injected intradermally into the abdomen of rabbits. After 72 hr, a well-defined, firm, raised nodule (about 1.0 by 1.5 cm) with an erythematous border was seen at the injection site. Suspensions of cell wall and cytoplasmic material were injected intradermally, and the lesions appeared only at the site of cell wall injection. The cell walls, which were then treated with trypsin, pepsin, and ribonuclease, again produced the characteristic lesion. These nodular dermal lesions persisted for a minimal time of 10 days. The enzymatically treated cell walls were then hydrolyzed with 1 n HCl, and such hydrolysis up to 1 hr failed to alter the toxic activity of the cell walls. Similar dermal nodular lesions were obtained by injection of enzymatically treated cell walls of strains of Staphylococcus aureus, Streptococcus groups B, C, E, F, K, Lactobacillus casei, and Actinomyces israelii. Treatment with hot and cold trichloroacetic acid solutions and proteolytic enzymes, or with formamide, yielded insoluble fractions which produced the characteristic nodular lesions. The size of the lesion resulting from injection of these fractions was proportional to the amount of the injected material. The active fraction, which does not appear susceptible to hydrolysis by lysozyme, is thought to be cell wall mucopeptide. Histological studies showed skin abscesses due to the toxic reaction; however, in addition to the acute inflammatory reaction, there was local eosinophilia.
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PMID:Toxic properties of the cell wall of gram-positive bacteria. 533

The postembedding immunoperoxidase staining technique for the localization of immunoglobulins (light and heavy chains) and of lysozyme has been successfully applied to epoxy-embedded human lymph nodes, after removal of the resin. Glutaraldehyde-containing fixatives appear to be suitable for the immunohistochemical localization of human immunoglobulins and lysozyme, provided that the masked antigenicity of these proteins is recovered by proteolytic digestion of the tissue sections using 0.4% pepsin or 0.1% trypsin. Nonglutaraldehyde-containing fixatives allow the immunolocalization of human immunoglobulins without any enzymatic pretreatment. This study shows that tissues routinely fixed in glutaraldehyde and embedded for ultrastructural investigations are actually suitable for immunohistochemical studies on human immunoglobulins and lysozyme.
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PMID:Immunohistochemical localization of human immunoglobulins and lysozyme in epoxy-embedded lymph nodes: effect of different fixatives and of proteolytic digestion. 617 82


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