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)

From experiments with glycoproteins containing the glycopeptide linkages, arabinose-O-hydroxyproline and galactose-O-serine (plant cell wall glycopeptides), N-acetylgalactosamine-O-serine/threonine (pig submaxillary mucin), and N-acetyl-glucosamine-N-asparagine (fetuin), it is apparent that anhydrous liquid HF, a reagent commonly used by snythetic peptide chemists for the complete removal of protecting groups from synthetic peptides, cleaves the O-glycosidic linkages of neutral sugars in 1 hr at 0 degrees C, and the O-glycosidic linkages of amino sugars in 3 hr at 23 degrees C. The N-glycosidic linkage of N-acetylglucosamine to asparagine is not cleaved under any conditions that have been tested. Sodium dodecyl sulfate gel electrophoresis of bovine serum albumin treated in HF does not show any degradation of peptide bonds. Some relatively stable enzymes (lysozyme and RNase) have been shown by others to retain most of their enzymic activity after short treatment (1 hr at 0 degrees C) in HF. With the specificity of HF at 0 degrees C for neutral sugars it should be possible to generate di- or trisaccharides in high yield from polysaccharides containing both neutral and amino sugars with neutral sugars as the reducing termini.
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PMID:A new approach to the structural determination of glycoproteins and polysaccharides: anhydrous HF solvolysis. 7 2

1. An enzyme that catalyzes hydrolysis of acetamido groups of chitin derivatives was found in the supernatant fraction of Mucor rouxii. 2. Partially O-hydroxyethylated chitin (glycol chitin) was used as a substrate in the purification and characterization of this enzyme. A 140-fold purification was obtained by means of ammonium sulfate fractionation followed by chromatography on carboxymethylcellulose and DEAE-cellulose. 3. The enzyme releases about 30% of the acetyl groups of glycol chitin, giving a product with a decreased sensitivity to lysozyme. The enzyme also deacetylates chitin and N-acetylchitooligoses, whereas it is inactive toward bacterial cell wall peptidoglycan, N-acetylated heparin, a polymer of N-acetylgalactosamine, di-N-acetylchitobiose and monomeric N-acetylglucosamine derivatives. 4. This enzyme shows a pH optimum of 5.5. The Km value for glycol chitin is 0.87 g/l or 2.6 mM with respect to monosaccharide residues. 5. The occurrence of this enzyme accounts for the formation of chitosan in fungi.
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PMID:A pathway of chitosan formation in Mucor rouxii. Enzymatic deacetylation of chitin. 24 Jun 96

Galactose, lactose, N-acetylgalactosamine, N-acetylglucosamine and fibrinoglycopeptides were bound to lysozyme by different linkages. These glycosylated lysozymes were tested as N-acetylneuraminic acid acceptors using particular sialytransferase preparations from frog and bovine liver and from bovine and porcine submandibular glands. Desialylated fetuin served as reference compound. Galactose residues of desialo-fetuin and lysozyme-lactose are sialylated by all four sialytransferases tested, galactose bound to lysozyme via a phenylazo group is inactive with the enzyme from bovine submandibular gland, and galactose bound directly to lysozyme serves as substrate only for the frog liver sialytransferase. Lysozyme-phenylazo-N-acetylgalactosamine is active only with the sialytransferase from bovine sumbandibular gland. N-Acetylglucosamine derivatives of lysozyme are inactive with all sialytransferases tested. These observations are discussed in the light of the natural substrates for the sialytransferases investigated.
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PMID:The specificity of sialytransferases using glycosylated lysozyme derivatives as substrates. 51 Oct 94

Previous findings have demonstrated the presence of muramic acid and the lack of sialic acid in gastropod glycoconjugates from different tissues. The present study investigated the composition of muramyl derivatives in Mollusca Gastropoda tissue from the foot, mantle and periesophageal ganglia, using HRP-labeled lectins (LTA, UEA I, GSA IB4, GSA II, DBA, SBA, RCA II, WGA, PNA, ConA) and glycosidase digestion (neuraminidase, lysozyme, alpha-L-fucosidase, beta-N-acetylglucosaminidase, alpha-N-acetylgalactosaminidase). Muramyl derivatives from the tissue examined showed some differences related to the composition of the terminal disaccharides. Indeed, foot and mantle mucocytes exhibited muramic acid in a terminal position, linked to (subterminal) N-acetylgalactosamine, whereas in neuron cells muramic acid was present in an internal position and linked to N-acetylglucosamine. Diversities also occurred between foot and mantle mucocytes with respect to the receptor sugar for penultimate N-acetylgalactosamine.
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PMID:Identification of muramyl derivatives in Mollusca Gastropoda tissue. 191 77

Fusobacterium nucleatum expresses lectinlike adherence factors which mediate binding to a variety of human tissue cells. Adherence is selectively inhibited by galactose, lactose, and N-acetyl-D-galactosamine. In this study, adherence of F. nucleatum to human peripheral blood polymorphonuclear neutrophils (PMNs) was investigated. The results indicated that the fusobacteria adhered to live and metabolically inactivated or fixed PMNs. Adherence of F. nucleatum resulted in activation of PMNs as determined by PMN aggregation, membrane depolarization, increased intracellular free Ca2+, superoxide anion production, and lysozyme release. Transmission electron micrographs showed that F. nucleatum was phagocytized by the PMNs. Microbicidal assays indicated that greater than 98% of F. nucleatum organisms were killed by PMNs within 60 min. Adherence to and activation of PMNs by F. nucleatum were inhibited by N-acetyl-D-galactosamine or lactose greater than galactose, whereas equal concentrations of glucose, N-acetyl-D-glucosamine, mannose, and fucose had little or no effect on F. nucleatum-PMN interactions. Pretreatment of the fusobacteria with heat (80 degrees C, 20 min) or proteases inhibited adherence to and activation of PMNs, but superoxide production was also stimulated by heated bacteria. The results indicate that interaction of F. nucleatum with PMNs is lectinlike and is probably mediated by fusobacterial proteins which bind to other human tissue cells. Adherence of F. nucleatum to PMNs in the absence of serum opsonins, such as antibodies and complement, may play an important role in PMN recognition and killing of F. nucleatum in the gingival sulcus and in the subsequent release of PMN factors associated with tissue destruction.
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PMID:Lectinlike interactions of Fusobacterium nucleatum with human neutrophils. 255 9

Binding of human lactoferrin (hLf) by purified rat liver plasma membranes was studied to clarify whether the liver possesses specific hLf receptors. The binding was rapid between 4 degrees and 37 degrees C, with a pH optimum close to 5.0. At 22 degrees C and in glycine-NaOH (5 mM, pH 7.4) containing 150 mM NaCl and 0.5% albumin, 1 microgram of membrane bound a maximum of 11.8 ng hLf. The dissociation constant of the interaction was 1.6 X 10(-7) M. Other proteins of high isoelectric points (lactoperoxidase, lysozyme, and particularly salmine sulfate) and a piperazine derivative inhibited hLf binding in a concentration-dependent manner. In contrast, monosaccharides (galactose, N-acetylgalactosamine, mannose, and fucose) were ineffective. By omitting NaCl from the incubation buffer, binding was increased 3.6-fold. Erythrocyte ghosts bound hLf less firmly and alveolar macrophages more firmly than hepatic plasma membranes. Liver cell fractionations performed after the intravenous injection of labeled hLf showed that approximately 88% of the hepatic radioligand was associated with parenchymal cells. When binding was expressed per unit of cell volume, however, more hLf was present in nonparenchymal than in parenchymal cells, implying that the above value was determined by the relative cell masses rather than affinities alone. It is concluded that the binding of hLf by hepatic plasma membranes is electrostatic, i.e., is mediated by the cationic nature of the ligand, and that it is explicable in terms of a "specific nonreceptor interaction" of the generalized type proposed by Cuatrecasas and Hollenberg (Adv. Protein Chem. 30: 251-451, 1976).
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PMID:Interaction of human lactoferrin with the rat liver. 298 44

The structure of polysaccharide prepared by lysozyme digestion from the cell wall of Propionibacterium acnes strain C7 was examined. The polysaccharide fraction was composed of glucose, galactose, mannose, galactosamine, and diaminomannuronic acid in a molar ratio of 1:1:0.3:1:2. By Smith degradation of the polysaccharide, diaminouronic acid-containing fractions were obtained, and the configuration of diaminouronic acid was identified as 2,3-diacetamido-2,3-dideoxymannuronic acid [Man(NAc)2A] by means of 1H-NMR and 13C-NMR spectroscopic analyses. The results of analyses involving methylation and partial acid hydrolysis led to the conclusion that the polysaccharide has the repeating unit----6)Gal(alpha 1----4)Man(NAc)2A(beta 1----6)Glc(alpha 1----4)Man(NAc)2A (beta 1----3)GalNAc(beta 1--. In addition, a portion of the galactose residues were substituted at C-4 by alpha 1----2 linked mannotriose.
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PMID:Structure of acidic polysaccharide from cell wall of Propionibacterium acnes strain C7. 403 Jul 44

1. After extraction of teichoic acid from cell walls of Bacillus licheniformis with dilute alkali, the insoluble residue contains the teichuronic acid and mucopeptide components and a small amount of residual phosphorus. 2. A complex of teichuronic acid and a part of the mucopeptide was isolated from the soluble fraction obtained by lysozyme treatment of alkali extracted walls. 3. Small-molecular-weight mucopeptide fragments, not containing teichuronic acid, are obtained from the soluble fraction in yields similar to those obtained after treatment of whole walls or acid-extracted walls with lysozyme. 4. The covalent linkages between teichuronic acid and mucopeptide are broken by treatment with dilute acid. The release of teichuronic acid chains is accompanied by the hydrolysis of N-acetylgalactosaminide linkages and the exposed N-acetylgalactosamine residues form chromogen under very mild conditions, indicating that they are substituted on C-3. 5. The initial rate of formation of reactive N-acetylgalactosamine residues during mild acid hydrolysis is parallel to the rate of extraction under the same conditions of teichuronic acid from alkali-treated insoluble walls, and to the rate of acid hydrolysis of glucose 1-phosphate. 6. The results suggest that the teichuronic acid chains are attached through reducing terminals of N-acetylgalactosamine residues to phosphate groups in the mucopeptide. 7. Muramic acid phosphate was isolated from the insoluble mucopeptide remaining after extraction of walls with dilute alkali followed by dilute acid.
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PMID:The cell wall of Bacillus licheniformis N.C.T.C. 6346. Linkage between the teichuronic acid and mucopeptide components. 541 40

1. The polysaccharide and mucopeptide components of the cell wall of Lactobacillus casei have been separated by mild conditions of acid hydrolysis. 2. Removal of the polysaccharide renders the mucopeptide susceptible to lysozyme. 3. The mucopeptide and polysaccharide components have been analysed and the results compared with those obtained previously. 4. The polysaccharides responsible for group specificity have a terminal reducing N-acetylgalactosamine residue substituted on C((3)) by the adjacent sugar; estimation of this component gave an indication of the molecular weight of the polysaccharides. 5. Evidence has been obtained for the presence of rhamnosyl-(1-->3)-N-acetylgalactosamine among the products of acid hydrolysis of the group B polysaccharide.
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PMID:Properties of the polysaccharide and mucopeptide components of the cell wall of Lactobacillus casei. 583 78

1. Four of the known components of wall preparations of vegative cells of Bacillus licheniformis N.C.T.C. 6346 have been isolated free of each other after successive treatments of the walls with trichloroacetic acid and lysozyme: (a) a mucopeptide consisting of glucosamine, muramic acid, alphain-diaminopimelic acid, glutamic acid and alanine in the molar proportions 1.0:0.8:1.0:1.2:1.7; (b) an insoluble protein; (c) teichoic acid containing phosphorus and glucose in equimolar amounts; (d) teichuronic acid containing equimolar amounts of N-acetylgalactosamine and glucuronic acid, as found by Janczura, Perkins & Rogers (1961). 2. Evidence has been obtained for the presence in the soluble fraction obtained by lysozyme treatment of whole walls of a stable covalent complex of the teichoic acid and the mucopeptide components. 3. The molar ratio of phosphorus to glucose in the teichoic acid present in intact walls or the soluble fractions obtained by extraction of the walls with lysozyme or trichloroacetic acid is 1.0:0.25, in contrast with values of about unity obtained for the purified teichoic acid. 4. Intact walls have been shown to contain polyribitol phosphate chains bearing different amounts of glucose substituents. 5. Trichloroacetic acid extracts of walls also contain polyribitol phosphate compounds of different chain lengths. Dialysis of trichloroacetic acid extracts removes the short chains of polyribitol phosphate that have been found to carry only very low amounts of glucose side chains. By contrast, the longer chains present in the non-diffusible fraction contain phosphorus and glucose in almost equimolar amounts.
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PMID:The isolation of structural components present in the cell wall of Bacillus licheniformis N.C.T.C. 6346. 586 10


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