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)

During a period commencing at birth and lasting for up to 27 months 193 milk samples have been collected from 29 mothers. The IgA globulin content was high immediately after birth, averaging 2.7 arb.U, decreasing to 0.3 arb.U within the first 2 to 3 weeks after birth, then remaining almost constant for the rest of the lactational period. In the case of IgG globulin, similar results were obtained, but the quantity was much smaller. IgM globulin was demonstrated in small quantities during the first 3 weeks of lactation. The lysozyme content varied considerably during the whole lactational period. Individual variations were found for all the immunoglobulins, while the concentration in the individual woman varied only slightly from day to day following in other respects the pattern described above. In 19 mothers IgA, IgG, IgM, lysozyme and electrolyte content were determined in serum and in milk from the right and the left breast on the same day. No difference in content was found between milk from the left and the right mammary gland. A positive correlation was found between the concentrations of IgA and sodium chloride in milk, between those of IgG in milk and serum, and between those of lysozyme in milk and serum. No variations were registered during the individual breast feeding, nor for the 24-hour period as a whole.
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PMID:Quantitative determination of immunoglobulins, lysozyme, and certain electrolytes in breast milk during the entire period of lactation, during a 24-hour period, and in milk from the individual mammary gland. 117 47

A porous silica of nominal 5 microns particle diameter and 30 nm pore size (Nucleosil 300-5) and a non-porous silica of nominal 1.5 microns particle diameter were activated with 3-mercaptopropyltriethoxysilane (MPTS), followed by the immobilization of the triazine dye, Cibacron Blue F3GA. Various biomimetic dye sorbents with graduated ligand densities between 1 mumol/m2 and 0.01 mumol/m2 were prepared. The capacities and the association constants associated with the binding of lysozyme to these sorbents were determined by frontal analysis experiments [J. Chromatogr., 476 (1989) 205-225]. Due to the ability of the Cibacron Blue F3GA-modified silicas to act as mixed mode coulombic and hydrophobic interaction sorbents and the highly charged nature of the surface structure of lysozyme (pl 11), two mobile phase conditions were examined. In one case a 0.1 M phosphate buffer, pH 7.8, was used as the equilibration and loading buffer, in the second case 1 M sodium chloride-0.1 M phosphate buffer, pH 7.8 was employed as the equilibration and loading buffer to monitor the influence of ionic interactions. The elution was performed in each case with a 2.5 M potassium thiocyanate solution. With the porous silica dye sorbents and 1 M NaCl present in the loading buffer, the highest capacity was achieved when Cibacron Blue F3GA was immobilised to the level of 0.1 mumol/m2. In the case of the non-porous silica dye sorbents, the maximum protein capacity was achieved when 0.5 mumol/m2 dye were immobilised onto the support. Evaluation of the frontal breakthrough curves confirmed that the kinetics of adsorption of lysozyme onto the non-porous sorbent were substantially faster than the adsorption of lysozyme onto the porous sorbent due to the absence of pore diffusion effects in case of the non-porous support. Furthermore, the adsorption of lysozyme on both sorbents was faster when no salt was added to the loading buffer, indicating that there is either conformational or reorientation effects operating during the specific binding of the protein to the dye ligand, or that the interaction is proceeding through the participation of a second class of binding sites. The magnitude of the association constants, Ka, for the lysozyme-Cibacron Blue F3GA systems were found to be dependent on the ligand density of the sorbent. With decreasing ligand density, the protein-ligand interaction became stronger, e.g. Ka values became larger. These results confirm earlier observations on the effect of ligand steric compression on the affinate-ligand association constant, e.g. the protein needs sufficient space to interact with the ligand in an optimum way.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:High-performance liquid chromatography of amino acids, peptides and proteins. CIX. Investigations on the relation between the ligand density of cibacron blue immobilized porous and non-porous sorbents and protein-binding capacities and association constants. 166 4

Crystals of bacteriophage T4 lysozyme used for structural studies are routinely grown from concentrated phosphate solutions. It has been found that crystals in the same space group can also be grown from solutions containing 0.05 M imidazole chloride, 0.4 M sodium choride, and 30% polyethylene glycol 3500. These crystals, in addition, can also be equilibrated with a similar mother liquor in which the sodium chloride concentration is reduced to 0.025 M. The availability of these three crystal variants has permitted the structure of T4 lysozyme to be compared at low, medium, and high ionic strength. At the same time the X-ray structure of phage T4 lysozyme crystallized from phosphate solutions has been further refined against a new and improved X-ray diffraction data set. The structures of T4 lysozyme in the crystals grown with polyethylene glycol as a precipitant, regardless of the sodium chloride concentration, were very similar to the structure in crystals grown from concentrated phosphate solutions. The main differences are related to the formation of mixed disulfides between cysteine residues 54 and 97 and 2-mercaptoethanol, rather than to the differences in the salt concentration in the crystal mother liquor. Formation of the mixed disulfide at residue 54 resulted in the displacement of Arg-52 and the disruption of the salt bridge between this residue and Glu-62. Other than this change, no obvious alterations in existing salt bridges in T4 lysozyme were observed. Neither did the reduction in the ionic strength of the mother liquor result in the formation of new salt bridge interactions. These results are consistent with the ideas that a crystal structure determined at high salt concentrations is a good representation of the structure at lower ionic strengths, and that models of electrostatic interactions in proteins that are based on crystal structures determined at high salt concentrations are likely to be relevant at physiological ionic strengths.
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PMID:Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. 206 26

Octadecyl-bonded silica, commonly used for reverse-phase high-pressure liquid chromatography, was modified using surfactants bearing ionizable groups and the modified packing used in ion-exchange chromatography of proteins. The surfactants 2-(n-hexadecylheptaethoxy)acetic acid, 1-(n-hexadecyloctaethoxy)ethylene-diamine, and N-(n-hexadecyloctaethoxy)pyridinium were adsorbed onto test columns packed with octadecyl-bonded silica particles. The proteins lysozyme, bovine serum albumin, trypsin, horse serum cholinesterase, and bovine liver carboxylesterase were used to study the ion-exchange characteristics of the modified packings. The retention order of the proteins on the surfactant-modified stationary phases were as predicted by the isoelectric point of each protein. In addition, the interaction of enzymes with the packings did not result in significant loss of enzymatic activity. Surfactant removal was possible with the use of organic solvents and this allowed the octadecyl-bonded surface to be used again in the reverse-phase mode. During the course of the experiments, no degradation in the packing's performance was observed due to loss of adsorbed surfactant, even after over 85,000 column volumes of sodium chloride and Tris-HCl buffers were circulated through the column.
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PMID:Reversible conversion of octadecyl-bonded silica to ion-exchange surfaces for protein separations. 254 Jun 75

The killing of Staphylococcus aureus strain 1030 and derived variants of it by lysozyme increased with increased lysozyme concentrations or decreased concentrations of sodium chloride. beta-Lactamase-producing and non-producing derivatives of strain 1030 were constructed. The former were less susceptible to lysozyme. Induction of beta-lactamase synthesis with 2-2'carboxyphenyl-benzoyl-6-penicillanic acid increased the resistance of producer strains to lysozyme. These results are discussed in relation to the spread of beta-lactamase-producing strains of S. aureus.
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PMID:The susceptibility to lysozyme of beta-lactamase-producing and non-producing derivatives of Staphylococcus aureus strain 1030. 349 26

The docking or polymerization of globular proteins is demonstrated to cause changes in proton NMR spin-lattice (T1) relaxation times. Studies on solutions of lysozyme, bovine serum albumin, actin, and tubulin are used to demonstrate that two mechanisms account for the observed changes in T1. Polymerization displaces the hydration water sheath surrounding globular proteins in solution that causes an increase in T1. Polymerization also slows the average tumbling rate of the proteins, which typically causes a contrary decrease in T1. The crystallization reaction of lysozyme in sodium chloride solution further demonstrates that the "effective" molecular weight can either decrease or increase T1 depending on how much the protein is slowed. The displacement of hydration water increases T1 because it speeds up the mean motional state of water in the solution. Macromolecular docking typically decreases T1 because it slows the mean motional state of the solute molecules. Cross-relaxation between the proteins and bound water provides the mechanism that allows macromolecular motion to influence the relaxation rate of the solvent. Fast chemical exchange between bound, structured, and bulk water accounts for monoexponential spin-lattice relaxation. Thus the spin-lattice relaxation rate of water in protein solutions is a complex reflection of the motional properties of all the molecules present containing proton magnetic dipoles. It is expected, as a result, that the characteristic relaxation times of tissues will reflect the influence of polymerization changes related to cellular activities.
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PMID:The influence of macromolecular polymerization of spin-lattice relaxation of aqueous solutions. 369 22

The deoxyribonucleic acid (DNA) of Streptococcus lactis C2, S. cremoris B(1), and S. diacetilactis 18-16 was labeled by growing cells in Trypticase soy broth containing (3)H-labeled thymine. The cells were gently lysed with lysozyme, ethylenediaminetetraacetic acid, and sodium lauryl sulfate. The chromosomal DNA was separated from plasmid DNA by precipitation with 1.0 M sodium chloride. The existence of covalently closed circular DNA in the three organisms was shown by cesium chloride-ethidium bromide equilibrium density gradient centrifugation of the cleared lysate material. In an attempt to correlate the loss of lactose metabolism with the loss of plasmid DNA, lactose-negative mutants of these organisms were examined for the presence of extrachromosomal particles. Covalently closed circular DNA was detected in the lactose-negative mutants of S. lactis C2 and S. diacetilactis 18-16. In S. cremoris B(1), however, no covalently closed circular DNA was observed by using cesium chloride-ethidium bromide gradients. Electron micrographs of the satellite band material from S. lactis C2 and its lactose-negative mutant confirmed the presence of plasmid DNA. Three distinct plasmids having approximate molecular weights of 1.3 x 10(6), 2.1 x 10(6), and 5.1 x 10(6) were observed in both organisms.
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PMID:Extrachromosomal elements in group N streptococci. 420 91

1. Nucleic acids were released from Escherichia coli by lysing with tri-iso-propylnaphthalene sulphonate and 4-aminosalicylate and then extracting with a phenol-cresol mixture. 2. Nucleic acids were similarly released from Bacillus subtilis after initial treatment with lysozyme. 3. DNA was sedimented after careful precipitation with m-cresol or 2-butoxyethanol (0.1-0.12vol.) in the presence of 20% sodium benzoate. 4. Contaminating ribosomal RNA was removed by precipitation in the presence of 4m-sodium chloride or by extracting DNA with an acetate-butyrate mixture, in which RNA is insoluble. 5. The DNA from B. subtilis has a transforming ability of 0.3-0.6% for the tryptophan marker. 6. Ribosomal RNA was then precipitated with rapidly labelled RNA by the addition of an equal volume of 2-butoxyethanol. 7. There was good separation of the nucleic acids from protein and polysaccharides.
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PMID:Isolation of deoxyribonucleic acid and ribosomal ribonucleic acid from bacteria. 496 18

Suspensions of enterococci were treated with lysozyme in the presence of osmotic stabilizers. The resulting osmotically fragile bodies prepared from Streptococcus faecium strain F24 and S. faecalis strain E1 gave rise to L-forms under optimal osmotic and nutritional conditions for treatment and subsequent growth. The most critical component of the growth medium, to obtain maximum yields, was the nature and concentration of the added salt. The two most effective salts were sodium chloride and ammonium chloride in the range of 2 to 3% (w/v) added to a suitable agar base. Ammonium chloride was more versatile, because it could be used with either sucrose or polyethylene glycol 4000 as the osmotic stabilizer for preparation and dilution of the osmotically fragile bodies. Sodium chloride would not consistently support growth of S. faecium F24 as L-forms when polyethylene glycol 4000 was used as the osmotic stabilizer during lysozyme treatment. Time-course studies of concurrent cell wall removal and L-form induction suggested that maximal induction required only cell wall damage rather than complete wall removal. This method for induction of L-forms from a suspension of enterococci is a significant improvement over other presently known methods.
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PMID:Induction of enterococcal L-forms by the action of lysozyme. 499 Aug 48

Suspensions of Streptococcus faecium, prepared by washing with and resuspending in water, were lysed slowly if sodium chloride was added prior to lysozyme; however, if brief incubation with lysozyme was followed by addition of sodium chloride, lysis was immediate and extensive. Relatively lysozyme-resistant strains of S. faecalis could be lysed readily by adding lysozyme first. The primary addition of lysozyme apparently resulted in a "sensitized" cell with a damaged wall, as evidenced by N-acetylhexosamine release. Anionic detergents could replace sodium chloride in lysing these sensitized cells. The difference in activity associated with the order of addition probably involved a competition for reactive sites on the cell surface.
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PMID:Differential lytic response of enterococci associated with addition order of lysozyme and anions. 537 Feb 73


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