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)

A murine monoclonal antibody, VM-1, which binds to basal cells of normal human epidermis, reduces the ability of human squamous cell carcinoma cells (SCL-1) derived from the skin to attach and spread on collagen by about 50% and causes cell rounding. Similar effects have been previously shown using normal human keratinocytes. The attachment of cell lines derived from human lung squamous cell carcinomas (SW1271 and SW900), melanoma A375, glioblastoma 126, and fibrosarcoma HT1080 is also inhibited by this antibody. VM-1 antibody does not bind to normal human fibroblasts, benign nevus cells, or the human B-cell-derived line 8866. VM-1 antibody inhibits the growth of SCL-1 cells in vitro as measured by cell numbers and [3H]thymidine ([3H]TdR) incorporation. It is not cytolytic in the presence of complement as measured by 51Cr release. Repeated treatment of SCL-1 cells with VM-1 antibody significantly reduces the proportion of SCL-1 cells that attach to collagen. In addition, after treatment of SCL-1 cells with VM-1 antibody, several proteins can no longer be demonstrated by gel electrophoresis of the cell-free supernatant. The VM-1 antibody effect on attachment and spreading is partially reversed by pretreatment of the collagen surface with laminin and fibronectin, but not with the carbohydrates chondroitin-6-sulfate or hyaluronic acid or with the protein lysozyme. By fluorescence staining, the antigen recognized by VM-1 antibody is membrane-bound and Triton X-100 extractable. The VM-1 antigen is excluded from Bio-Sil TSK-400 and sediments at about 10.5 S. It has a covalent molecular weight on the order of 10(6). Proteinase K digestion produces VM-1 antibody reactive fragments, assumed to be polysaccharides, with a polydisperse molecular weight distribution in the range 5000 to 30,000. The VM-1 antigen is partially lost from solution on boiling and is no longer detectable in the aqueous or organic phase after chloroform-methanol extraction. The properties of the VM-1 antigen are consistent with those of a proteoglycan involved in attachment and spreading of keratinocytes and certain tumor cells on collagen.
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PMID:Inhibition of attachment and growth of tumor cells on collagen by a monoclonal antibody. 369 49

Membranes were isolated from Bacillus stearothermophilus 2184D by lysozyme digestion of the cell wall and subsequent differential centrifugation. Observations with the electron microscope indicate that such membranes are relatively intact and have a typical membrane appearance. Nitrate will preferentially oxidize the cytochrome b of such membranes. Approximately 80% of the total respiratory nitrate reductase activity of whole cells can be localized in the washed membrane fraction and the process of membrane isolation results in a sixfold purification of this enzyme. Of several detergents tested, sodium dodecyl sulfate, Triton 114, and Triton X-100 are most effective in converting reduced methyl viologen-nitrate reductase to a form which will not pellet at 130,000 x g. Density gradient analysis reveals that such detergent-mediated solubilization converts virtually all membrane protein to a form of lighter density.
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PMID:Localization and solubilization of the respiratory nitrate reductase of Bacillus stearothermophilus. 433 9

Transformation of R-factor RP4 specifying resistance to ampicillin, kanamycin, and tetracycline from Escherichia coli to Rhizobium trifolii is reported. Partially purified RP4 deoxyribonucleic acid (DNA) of the donor strain E. coli J5-3 that carried the R-factor was prepared by the lysozyme-ethylenediaminetetraacetic acid-Triton X-100 procedure and was used in transformation experiments with R. trifolii as recipient. The frequency of transformation of the R-factor into R. trifolii was 1.3 x 10(-4). Dye buoyant density and sucrose gradient centrifugation of R. trifolii DNA showed that the expression of the specified drug resistance of RP4 by R. trifolii was accompanied by the acquisition of an extrachromosomal, satellite DNA component which has indistinguishable physical properties from the R-factor in the donor strain. The significance of the transformation is discussed.
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PMID:Transformation and physical properties of R-factor RP4 transferred from Escherichia coli to Rhizobium trifolii. 458 1

A procedure is described for the purification of bacterial flagella in the form of a filament-hook-basal body complex (intact flagella) free from detectable cell wall, membrane, or cytoplasmic material. Spheroplasts produced with lysozyme and ethylenediaminetetraacetic acid were lysed with Triton X-100, and the flagella were purified by (NH(4))(2)SO(4) precipitation, differential centrifugation, and CsCl gradient centrifugation. As much as 40% of the flagella were recovered, and they contained about one basal body per 4 to 6 mum of flagella. The same procedure developed for Escherichia coli was also successful for purifying intact flagella from Bacillus subtilis.
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PMID:Purification of intact flagella from Escherichia coli and Bacillus subtilis. 499 24

Extraction of a partially purified preparation of cell walls from Escherichia coli with the nonionic detergent Triton X-100 removed all cytoplasmic membrane contamination but did not affect the normal morphology of the cell wall. This Triton-treated preparation, termed the "Triton-insoluble cell wall," contained all of the protein of the cell wall but only about half of the lipopolysaccharide and one-third of the phospholipid of the cell wall. This Triton-insoluble cell wall preparation was used as a starting material in an investigation of several further treatments. Reextraction of the Triton-insoluble cell wall with either Triton X-100 or ethylenediaminetetraacetic acid (EDTA) caused no further solubilization of protein. However, when the Triton-insoluble cell wall was extracted with a combination of Triton X-100 and EDTA, about half of the protein and all of the remaining lipopolysaccharide and phospholipid were solubilized. The material which remained insoluble after this combined Triton and EDTA extraction still retained some of the morphological features of the intact cell wall. Treatment of the Triton-insoluble cell wall with lysozyme resulted in a destruction of the peptidoglycan layer as seen in the electron microscope and in a release of diaminopimelic acid from the cell wall but did not solubilize any cell wall protein. Extraction of this lysozyme-treated preparation with a combination of Triton X-100 and EDTA again solubilized about half of the cell wall protein but resulted in a drastic change in the morphology of the Triton-EDTA-insoluble material. After this treatment, the insoluble material formed lamellar structures. These results are interpreted in terms of the types of noncovalent bonds involved in maintaining the organized structure of the cell wall and suggest that the main forces involved are hydrophobic protein-protein interactions between the cell wall proteins and to a lesser degree a stabilization of protein-protein and protein-lipopolysaccharide interactions by divalent cations. A model for the structure of the E. coli cell wall is presented.
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PMID:Effect of ethylenediaminetetraacetic acid, Triton X-100, and lysozyme on the morphology and chemical composition of isolate cell walls of Escherichia coli. 500 Dec 5

Alysiella bovis adheres to surfaces by means of short, ruthenium red-staining, rod-like fimbriae. The fimbriae remain associated with the cell envelope of A. bovis, even when sonicated or exposed sequentially to toluene, Triton X-100, lysozyme, ribonuclease, and deoxyribonuclease. Adhesion of outer membrane-derived cell wall ghosts of A. bovis to glass was inhibited by IO4-, sodium dodecyl sulfate, urea, pronase, and trypsin. Protease treatment digested the fimbriae from the distal end, and exposure to sodium dodecyl sulfate depolymerized the fimbriae. Exposure of ghosts to 1% sodium dodecyl sulfate preferentially solubilized a 16,500-dalton protein which was subsequently purified by gel filtration and demonstrated to be a glycoprotein (ca. 17% carbohydrate). Antibodies raised against the 16,500-dalton glycoprotein agglutinated whole cells and inhibited adhesion of ghosts to glass.
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PMID:Mechanism of adhesion of Alysiella bovis to glass surfaces. 620 60

Bacteriophage T4 particle-associated lysozyme, purified to electrophoretic homogeneity, was found to be a protein with a relative molecular mass of 15000. The lysozyme was purified from the particles of bacteriophage T4 e mutant and from the lysates of the 5tsl e T4 mutant, in which the enzyme is in soluble form. In the purification procedure advantage was taken of the affinity of the enzyme for GlcNAc-MurNac-LAla-DGlu-msA2pm-DAla (C6 muropeptide), one of the products of the digestion of Escherichia coli murein with lysozyme. The test for the quick estimation of bacteriolytic activity of the enzyme, using E. coli B freeze-dried cells, is described. The pH optimum of the particle-associated lysozyme was equal to about 6.0, ionic strength optimum to 0.05-0.1 M, and optimum Triton X-100 concentration to 1%, when this substrate was used. Some of the aspects of the possible biological significance of the particle-associated lysozyme in bacteriophage T4 infection are discussed.
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PMID:Purification and some properties of bacteriophage T4 particle-associated lysozyme. 634 57

The attacins are antibacterial proteins which accumulate in the hemolymph of the giant silk moth, Hyalophora cecropia, in response to a bacterial infection. Here we show that the permeability barrier function of the outer membrane is affected shortly after addition of attacin to growing cultures of Escherichia coli. Specifically, the penetration through the outer membrane of beta-lactam antibiotics, chicken egg white lysozyme and the detergent Triton X-100 was found to be facilitated. The sensitivity of E. coli to cecropin B, another antibacterial protein present in the hemolymph of H. cecropia, was also found to be increased after treatment with attacin. The results suggest that the target of the attacins in E. coli is the outer membrane. Other effects of the attacins which have been observed are likely to be indirect consequences of the alteration in the properties of the outer membrane. These effects include changes in the cell shape, irregular patterns of cell division and lysis. The minimal concentration at which the attacins affected the growth of E. coli was 1 and 0.5 microM for the neutral (pI 7) and basic (pI 9) attacins, respectively, which corresponds to less than 2% of the concentration of the attacins in the hemolymph of infected pupae.
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PMID:The antibacterial effect of attacins from the silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli. 639 89

Polypeptide and polysaccharide outer membrane components of Brucella abortus 99 (S) were investigated by analysis of cell-wall fractions by sodium dodecyl-sulfate polyacrylamide gel electrophoresis and staining with coomassie blue and periodic acid silver stain. Crude cell-walls were deprived by Triton X-100 treatment of most cytoplasmic material as seen by electron microscopy and cytochrome determination (cell-walls). They were submitted to hot SDS to obtain intentionally after centrifugation, peptidoglycan in the insoluble fraction: SDS-I fractions or peptidoglycan sacculi, and outer membrane components in the SDS soluble fraction as for Enterobacteriaceae. The SDS-soluble fraction contained two major components: a high molecular weight broad band of smooth lipopolysaccharide (S-LPS) and a 43k polypeptide band. The SDS-I fractions were treated by lysozyme to solubilize peptidoglycan before analysis. They contained two major polypeptide groups 36-37-38k, 25-26-27k, a minor one at 31k and variable amounts of high molecular weight S-LPS. The polypeptide and polysaccharide patterns of the entire outer membrane obtained from lysozyme hydrolysed cell-walls are the sum of both SDS soluble and insoluble fraction patterns. These results mean that 25-27k and 36-38k bands are strongly bound to peptidoglycan, probably covalently. The 25-26-27k bands heavily stained for polysaccharides would be glycopolypeptides. In addition, the polysaccharide patterns of S-LPS fraction appears as a high molecular weight broad band, contrary to the multiple regularly spaced bands of high molecular weight E. coli S-LPS. The B. abortus outer membrane is composed of four major components: LPS, 43k and 36-37-38k polypeptides and 25-26-27k glycopeptides.
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PMID:Evidence of three major polypeptide species and two major polysaccharide species in the Brucella outer membrane. 641 68

Purified disaccharide peptide monomers obtained from Neisseria gonorrhoeae by enzymatic digestion of gonococcal peptidoglycan damaged the mucosa of human fallopian tubes in organ culture. Two peptidoglycan fragments were tested: a nonreducing, anhydromuramyl-containing monomer (the principal fragment shed by growing gonococci) and the analogous reducing, muramidase-derived monomer. The damage produced by either of these peptidoglycan monomers resulted in sloughing of ciliated cells from the mucosa and resembled the damage observed in active gonococcal infection and that produced by filter-sterilized toxic supernatant fluids from gonococcal-infected organ cultures. The minimal toxic dose of peptidoglycan monomers was 0.75 micrograms/ml. Neither lipopolysaccharide, sodium dodecyl sulfate, nor Triton X-100, possible contaminants from the monomer-purification procedures, was present in sufficient quantity to account for the damage. Both of the gonococcal peptidoglycan monomers may be present in vivo and thus may play a role in the pathogenesis of gonococcal infection.
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PMID:Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian-tube mucosa. 642 21


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