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)

The interaction between human breast milk macrophages and lactoferrin (LF) in its native form was studied in in vitro culture. Competitive inhibition-binding studies with 125I-LF and unlabeled LF showed that a specific receptor for LF was present on breast milk macrophages. LF at concentrations of 10(-6) -10(-9)M resulted in a dose-dependent inhibition of prostaglandin E2 secretion by breast milk macrophages (control-45 +/- 7; LF 10(-6)M -9 +/- 1 ng/ml/10(6) cells). This inhibitory effect was also observed when the macrophages were stimulated with Concanavalin A (LF 10(-6) M -80 +/- 5; 10(-9) M -45 +/- 8% inhibition of prostaglandin E2 secretion by Concanavalin A stimulated macrophages). Lactalbumin and lactoglobulin had no effect. Similar concentrations of LF had no effect on lysozyme production. We also demonstrated that human milk macrophages are capable of eliciting an oxidative burst as measured by superoxide or hydrogen peroxide production when stimulated by phorbol myristate acetate in in vitro culture. (basal superoxide -1.4 +/- 0.3; phorbol myristate acetate 28.8 +/- 3.5 nmol/1 X 10(6) cells/90 min; basal hydrogen peroxide 11.7 +/- 4.6; phorbol myristate acetate -57.5 +/- 2.3 nmol/mg protein/90 min). LF had no effect on the oxidative burst. These results suggest that interaction of aqueous and cellular components of breast milk may occur and result in varied physiological effects.
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PMID:Lactoferrin inhibits prostaglandin E2 secretion by breast milk macrophages. 302 5

Proton release by flash excitations was measured with right-side-out vesicles prepared from Rhodopseudomonas sphaeroides by lysozyme-EDTA treatment followed by hypotonic treatment. Absorbance change at 586 nm in the presence of bromcresol purple was measured to monitor the pH change. In the presence of horse heart cytochrome c, which catalyzes the electron transfer from the cytochrome b-c1 complex to the primary electron donor, the single-turnover flash elicited release of about two protons per primary electron donor, which was rereduced rapidly by the added cytochrome c. The halftime of the proton release was about 70 ms at pH 6.3 and at a redox potential of about 150 mV. The rate was considerably lower than that of the electron transfer from the cytochrome b-c1 complex to cytochrome c. However, multiple flashes with intervals of 60 ms caused release of the same amount of protons as that by flashes with longer intervals. This indicated that the proton release itself was rapid, but delocalization was slower. Antimycin A inhibited the proton release, and myxothiazol almost completely abolished it.
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PMID:Flash-induced proton release in Rhodopseudomonas sphaeroides spheroplasts. 303 25

Two millimeter range ESR-spectroscopy was used to measure the values of magnetic resonance parameters of egg lysozyme samples modified with nitroxyl label 4-(iodine-acetamide)-2,2,6,6-tetramethylpiperidine-1-oxyl by hist-15 residue. It has been shown that in a lyophilic sample the spin label forms a hydrogen bond with the protein group and when the sample is moistened--with water molecules. Temperature changes of the pattern of ESR line are analysed. It is concluded that in the moistened samples within 230-320 K the nitroxyl fragment of the label gets engaged in anisotropic movement with preferable rotation around Z-axis of N-O. fragment with anisotropy coefficient 5 and mean correlation time tau congruent to 5 X 10(-7) divided by 5 X 10(-8) c.
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PMID:[Study of lysozyme by a spin-label method in the 2-mm range]. 303 34

Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.
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PMID:Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. 311 11

The effects of clofazimine on phagocyte functions associated with antimicrobial activity have been investigated. Clofazimine at a variety of concentrations was capable of enhancing the spontaneous production of hydrogen peroxide and the intracellular killing ability of phagocytes; but had no effect on resting phagocyte lysozyme release, or hexose monophosphate shunt (HMPS) activity. However, when these latter functions were assessed in the presence of a phagocytic stimulus, clofazimine moderately increased both lysozyme release and HMPS activity. A 25 Kd glyco-lipoprotein derived from Mycobacterium tuberculosis has been shown to inhibit these antimicrobial functions. Clofazimine was capable of partially reversing the inhibitory effect of the mycobacterial component in all of the systems assessed. Partial restoration was observed at concentrations of 0.5 mg/l and was maximal at 2 mg/l. These studies indicate important mechanisms operative in the pathogenesis of tuberculosis and suggest that clofazimine may have clinical relevance in the treatment of mycobacterial diseases.
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PMID:Clofazimine reverses the inhibitory effect of Mycobacterium tuberculosis derived factors on phagocyte intracellular killing mechanisms. 312 22

Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.
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PMID:Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. 320 Mar 17

A combination of ab initio calculations, "knowledge-based prediction", molecular graphics and site-directed mutagenesis has enabled us to probe the molecular details of antibody:antigen recognition and binding and to alter the affinity and specificity of an antibody for its antigen. The significance of electrostatic hydrogen bonding, hydrophilic/hydrophobic patch matching and van der Waals interactions as well as CDR:CDR interactions are discussed in relation to the results of site-directed mutagenesis experiments on the anti-lysozyme antibody Gloop2. The ability to generate reconstructed antibodies, chimeric antibodies, catalytic antibodies and the use of modelled antibodies for the design of drugs is discussed.
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PMID:Engineering antibody affinity and specificity. 320 95

A single intraperitoneal injection of cisplatin (10 mg/kg body weight) in C3H/He mice increases the total number of peritoneal exudate cells (PEC) and macrophages (m phi) within 24 to 48 h. The total number of PEC from untreated mice ranged from 4 to 5 x 10(6) cells/ml containing 2.5 to 3 x 10(6) macrophages, whereas in cisplatin treated mice total number of PEC ranged up to 25 x 10(6) cells/ml. These PEC contained up to 16 x 10(6) m phi. The macrophages obtained from cisplatin injected mice show enhanced cytotoxicity, cytostasis and binding to Dalton's lymphoma cells in vitro. These activated macrophages release into the culture medium factors having cytolytic and cytostatic effect on Dalton's lymphoma cells. The activated macrophages also show enhanced capacity to release superoxide anions, hydrogen peroxide, lysozyme, arginase and interleukin-1.
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PMID:In vivo activation of murine peritoneal macrophages by intraperitoneal administration of cisplatin. 326 18

Assignments for 1H NMR resonances of 121 of the 129 residues of hen egg white lysozyme have been obtained by sequence-specific methods. Spin systems were identified with phase-sensitive two-dimensional (2-D) correlated spectroscopy and single and double relayed coherence transfer spectroscopy. For key types of amino acid residues, particularly alanine, threonine, valine, and glycine, complete spin systems were identified. For other residues a less complete definition of the spin system was found to be adequate for the purpose of sequential assignment. Sequence-specific assignments were achieved by phase-sensitive 2-D nuclear Overhauser enhancement spectroscopy (NOESY). Exploitation of the wide range of hydrogen exchange rates found in lysozyme was a useful approach to overcoming the problem of spectral overlap. The sequential assignment was built up from 21 peptide segments ranging in length from 2 to 13 residues. The NOESY spectra were also used to provide information about the secondary structure of the protein in solution. Three helical regions and two regions of beta-sheet were identified from the NOESY data; these regions are identical with those found in the X-ray structure of hen lysozyme. Slowly exchanging amides are generally correlated with hydrogen bonding identified in the X-ray structure; a number of exceptions to this general trend were, however, found. The results presented in this paper indicate that highly detailed information can be obtained from 2-D NMR spectra of a protein that is significantly larger than those studied previously.
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PMID:Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. 334 24

The mass density of protein crystals can be measured in Ficoll gradients as a function of hydrostatic pressure. Carbon tetrachloride-toluene mixtures provide convenient density markers, and the compressibility of these standards is reported. Measurements on tetragonal crystals of hen egg-white lysozyme yielded densities at room temperature of 1.2367(+/- 0.0010) g cm-3 at 1 atm and 1.2586(+/- 0.0017) g cm-3 at 1000 atm (1 atm = 101,325 Pa). When combined with the unit cell dimensions at these two pressures these values lead to an estimated compression (fractional change in volume) of the crystal solvent at 1000 atm of 0.0369(+/- 0.0054). This value is comparable to that of a 0.7 M solution of NaCl. From an approximate estimate of the Donnan effect for the crystal in the 1.4 M-NaCl mother liquor, the crystal solvent contains 0.8 M-Na+ and 2.5 M-Cl-. It is concluded that the compressibility of solvent in lysozyme crystals is, within experimental error, the same as bulk solvent and does not exhibit the dramatically altered compressibility expected of an ice or glass-like solid. The crystallographically observable water sites, 151 at 1 atm and 163 at 1000 atm, showed a tendency to increase the number of hydrogen bonds made to other water sites at the expense of hydrogen bonds made to protein. The explanation for this phenomenon is presently unknown. Water sites that occur in both structures tend to have comparable temperature factors and show some tendency to follow the pressure-induced changes in protein atom positions. The compression expected for the water molecules themselves is too small to be observable at the resolution of the X-ray data collected in this study.
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PMID:Effect of hydrostatic pressure on the solvent in crystals of hen egg-white lysozyme. 337 35


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