Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This paper relates to the efficacy of a catalytic converter in reducing the levels of certain pollutants emitted from an automobile engine and to the reduction and/or elimination of gross biologic damages in animals exposed to emissions from an exhaust system containing such catalysts. Groups of rats were exposed to diluted emissions from an automobile engine with and without catalyst. Concomitantly, a comparative experiment was conducted by exposing a group of rats to carbon monoxide alone (575 mg/m3). The parameters measured included hematocrit, serum LDH, GOT, and lysozyme. An elevation in hematocrit was observed in animals of the experiment run without catalyst and in those exposed to carbon monoxide; the use of the catalyst reduced the carbon monoxide levels in the exposure chambers by more than tenfold and prevented these bioeffects from occurring. Serum LDH activity was elevated in the groups of rats in the experiment conducted without catalyst, but no alternation was observed in the animals from the experiment utilizing the catalyst or in those exposed to carbon monoxide alone. The data obtained in this study showed that acute exposure to noncatalytic emissions caused significant alterations in certain biologic parameters. Conversely, the introduction of an oxidizing catalytic converter into the engine exhaust system reduced or prevented such biologic damage.
 ...
PMID:Biologic effects of auto emissions. I. Exhaust from engine with and without catalytic converter. 5 66

The aromatic regions in proton-decoupled natural abundance 13C Fourier transform nuclear magnetic resonance spectra (at 14.2 kG) of small native proteins contain broad methine carbon bands and narrow nonprotonated carbon resonances. Some factors that affect the use of natural abundance 13C Fourier transform NMR spectroscopy for monitoring individual nonprotonated aromatic carbon sites of native proteins in solution are discussed. The effect of protein size is evaluated by comparing the 13C NMR spectra of horse heart ferrocytochrome c, hen egg white lysozyme, horse carbon monoxide myoglobin, and human adult carbon monoxide hemoglobin. Numerous single carbon resonances are observed in the aromatic regions of 13C NMR spectra of cytochrome c, lysozyme, and myoglobin. The much larger hemoglobin yields few resolved individual carbon resonances. Theoretical and some experimental values are presented for the natural linewidths (W), spin-lattice relaxation times (T1), and nuclear Overhauser enhancements (NOE) of nonprotonated aromatic carbons and Czeta of arginine residues. In general, the 13C-1H dipolar mechanism dominates the relaxation of these carbons. 13C-14N dipolar relaxation contributes significantly to 1/T1 of C epsilon2 of tryptophan residues and Czeta of arginine residues of proteins in D2O. The NOE of each nonprotonated aromatic carbon is within experimental error of the calculated value of about 1.2. As a result, integrated intensities can be used for making a carbon count. Theoretical results are presented for the effect of internal rotation on W, T1, and the NOE. A comparison with the experimental T1 and NOE values indicates that if there is internal rotation of aromatic amino acid side chains, it is not fast relative to the over-all rotational motion of the protein.
 ...
PMID:Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Relaxation behavior. 16 39

Natural abundance 13C Fourier transform NMR spectra (at 15.18 MHz, in 20-mm sample tubes) of aqueous native proteins yield numerous narrow single carbon resonances of nonprotonated aromatic carbons. Techniques for the assignment of these resonances are presented. Each technique is applied to one or more of the following proteins: ferricytochrome c from horse heart and Candida krusei, ferrocytochrome c and cyanoferricytochrome c from horse heart, lysozyme from hen egg white, cyanoferrimyoglobins from horse and sperm whale skeletal muscle, and carbon monoxide myoglobin from horse. In all of the protein spectra we have examined, methine aromatic carbons give rise to broad bands. Studies of the narrow resonances of nonprotonated aromatic carbons of proteins are facilitated by removal of these broad bands by means of the convolution-difference method, preferably from spectra recorded under conditions of noise-modulated off-resonance proton decoupling. We present a summary of the chemical shift ranges for the various types of nonprotonated aromatic carbons of amino acid residues and hemes of diamagnetic proteins, based on our results for hen egg white lysozyme, horse heart ferrocytochrome c, horse carbon monoxide myoglobin, and carbon monoxide hemoglobins from various species...
 ...
PMID:Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy. Strategies for assignments. 16 40

The activity of serum angiotensin converting enzyme (ACE) was repeatedly measured together with serum lysozyme (LZM) in patients with untreated sarcoidosis. Changes in the clinical picture were registered using chest X-ray, forced vital capacity (FVC), diffusing capacity for carbon monoxide (DLCO) and appearance of extrapulmonary lesions. During a clinically unchanged period the highest ACE activity and the corresponding LZM value (not the highest value) were used for the calculation. A statistically significant change in ACE was noted when a normal chest X-ray changed to a stage II lesion or vice versa, and when a signficant change in FVC occurred. All other changes were insignificant. On the other hand, statistically significant changes in ACE were found during stable periods according to chest X-ray, FVC or DLCO. ACE is frequently elevated in serum of patients with active sarcoidosis. The fluctuations in activity mostly parallel the clinical course of the disease. The behaviour and metabolism of the enzyme need further investigation. An increased concentration of serum LZM is frequent in patients with active sarcoidosis. The highest LZM values are not always seen simultaneously with the highest ACE values, indicating that they probably express different dimensions of the disturbances in the sarcoid granuloma.
 ...
PMID:Angiotensin converting enzyme. III. Changes in serum level as an indicator of disease activity in untreated sarcoidosis. 23 19

Incubating and shaking Staphylococcus aureus in liquid whole egg causes a decline in viability. During the period of agitation, the natural pH of the egg rises from about 7.2 to between 8.0 and 8.2 as a result of a loss of carbon dioxide. However, if the pH of the egg is prevented from rising, either by not shaking or by addition of a buffer, S. aureus will grow. The cause of death is traced to the presence of lysozyme of egg white. Interestingly, the action of lysozyme is not attributable to its bacterial lytic property but, instead, to the basicity of the lysozyme molecule. This conclusion is supported by the fact that the lytic property of lysozyme is known to have its optimal activity near neutrality and by the finding that protamine sulfate, a nonenzymatic basic polypeptide, also caused death of S. aureus at pH 8.0 but not at 7.0. It was postulated that the rise in pH renders the bacterial cells more negatively charged, so that in the presence of positively charged molecules like lysozyme or protamine sulfate a complex is formed, agglutinating the cells.
 ...
PMID:Death of Staphylococcus aureus in liquid whole egg near pH 8. 23 29

Lysozyme activity of 403 strains of lactobacilli were investigated; of these 26 were from foreign sets and 377 were isolated from the contents of the stomach, feces and vaginal discharge of healthy adults. The species reference of lactobacillae was confirmed by the results of study of their physiologo-biochemical properties with the aid of 45 tests. A method of agar plates was adapted to determination of lysozyme: the autoclaved suspension of Micrococcus lysodeikticus (strain No. 2665) was added to the agar medium MPC-I, and lactobacilli were cultivated for 4 days in the CO2 atmosphere at 37 degrees C. There was revealed the capacity of L. fermenti and L. brevis to produce lysozyme; in L. fermenti the lysozyme activity was much more frequent (p less than 0.001); strains of the rest of the species of lactobacilli differentiated by the Rogosa and Sharpe's classification proved to be lysozyme-negative. It was shown that the lactobacilli of the L. fermenti species, included into the microflora of the intestine and the vagina of healthy adults as a rule possessed lysozyme activity. L. fermenti strain 90T-S4 used in the production of dry lactobacterin also produced lysozyme. All this favours an important role of L. fermenti in the protective function of the microflora.
 ...
PMID:[Ability of lactobacilli in the human microflora to produce lysozyme]. 81 10

In order to identify the functional groups which really contribute to the carbon dioxide gas adsorption by proteins, epsilon-amino groups of lysine residues of egg albumin were chemically modified with trinitrobenzene sulfonic acid to various degrees. About 60% of the total amount of carbon dioxide gas absorbed by solid egg albumin diminished by complete modification. The amount of carbon dioxide gas adsorbed by lysozyme, its hydrolyzates and gelatin hydrolyzates depended upon the lysine content, arginine content and average molecular weight. The good correlation was obtained between the amount of carbon dioxide gas absorbed and the total of lysine and arginine content of them. The ability of carbon dioxide gas adsorption by alpha-amino group of amino acids and oligopeptides was found to be developed by the elongation of the peptide chain of glycine and other amino acid, by the removal of alpha-carboxyl group of histidine and tyrosine to corresponding amines and by the esterification of alpha-carboxyl group of leucine with p-nitrophenol. These results clearly indicate that CO2 binding sites in protein in the gas-solid phase system are epsilon-amino, alpha-amino and guanidinium groups.
 ...
PMID:Identification and properties of reactive sites in protein capable of binding carbon dioxide in a gas-solid phase system. 87 81

The aim of this study was to explore whether amounts of angiotensin converting enzyme (ACE) and lysozyme produced within the lungs correlate more closely than serum levels of these enzymes, or other inflammatory markers, with chest radiographic profusion scores, lung function and therapy response in patients with pulmonary sarcoidosis. We have studied 25 patients, and levels in bronchoalveolar lavage (BAL) were used to determine "local" enzyme production by reference to serum and lavage albumin. Before treatment, serum lysozyme levels were elevated in more patients (80%) than serum ACE levels (40%). They also gave the best overall correlation with clinical measurements prior to treatment and falls in serum lysozyme closely parallelled improvement in lung function (transfer factor for carbon monoxide (DLCO)) on therapy. The only other markers showing significant correlations with disease severity were lavage neutrophil counts per ml and "local" ACE measurements prior to treatment. The value of pre-treatment levels of the different inflammatory markers in predicting response to corticosteroid therapy was explored and the only significant finding was that BAL lymphocyte percentages and numbers.ml-1 were initially higher in patients with lower post-treatment chest X-ray scores (p less than 0.01 and p less than 0.05, respectively). We conclude that serum lysozyme levels appear to be a more useful marker of overall disease activity in sarcoidosis than measurements of other inflammatory markers. However, BAL lymphocyte counts were the best predictive marker of radiographic response to corticosteroids.
 ...
PMID:Lavage versus serum measurements of lysozyme, angiotensin converting enzyme and other inflammatory markers in pulmonary sarcoidosis. 196 6

Solvent exchange of 18O-labeled buried water in bovine pancreatic trypsin inhibitor (BPTI), trypsin, and trypsin-BPTI complex is measured by high-precision isotope ratio mass spectrometry. Buried water is labeled by equilibration of the protein in 18O-enriched water. Protein samples are then rapidly dialyzed against water of normal isotope composition by gel filtration and stored. The exchangeable 18O label eluting with the protein in 10-300 s is determined by an H2O-CO2 equilibration technique. Exchange of buried waters with solvent water is complete before 10-15 s in BPTI, trypsin, and BPTI-trypsin, as well as in lysozyme and carboxypeptidase measured as controls. When in-exchange dialysis and storage are carried out at pH greater than or equal to 2.5, trypsin-BPTI and trypsin, but not free BPTI, have the equivalent of one 18O atom that exchanges slowly (after 300 s and before several days). This oxygen is probably covalently bound to a specific site in trypsin. When in-exchange dialysis and storage are carried out at pH 1.1, the equivalent of three to seven 18O atoms per molecule is associated with the trypsin-BPTI complex, apparently due to nonspecific covalent 18O labeling of carboxyl groups at low pH. In addition to 18O exchange of buried waters, the hydrogen isotope exchange of buried NH groups H bonded to buried waters was also measured. Their base-catalyzed exchange rate constants are on the order of NH groups that in the crystal are exposed to solvent (static accessibility greater than 0) and hydrogen-bonded main chain O, and their pH min is similar to that for model compounds. The pH dependence of their exchange rate constants suggests that direct exchange with water may significantly contribute to their observed exchange rate.
 ...
PMID:Solvent exchange of buried water and hydrogen exchange of peptide NH groups hydrogen bonded to buried waters in bovine pancreatic trypsin inhibitor. 244 53

Functionally intact plasma membranes were isolated from the cyanobacterium (blue-green alga) Anacystis nidulans through French pressure cell extrusion of lysozyme/EDTA-treated cells, separated from thylakoid membranes by discontinuous sucrose density gradient centrifugation, and purified by repeated recentrifugation. Origin and identity of the chlorophyll-free plasma membrane fraction were confirmed by labeling of intact cells with impermeant protein markers, [35S]diazobenzenesulfonate and fluorescamine, prior to membrane isolation. Rates of oxidation of reduced horse heart cytochrome c by purified plasma and thylakoid membranes were 90 and 2 nmol min-1 (mg of protein)-1, respectively. The cytochrome oxidase in isolated plasma membranes was identified as a copper-containing aa3-type enzyme from the properties of its redox-active and EDTA-resistant Cu2+ ESR signal, the characteristic inhibition profile, reduced minus oxidized difference spectra, carbon monoxide difference spectra, photoaction and photodissociation spectra of the CO-inhibited enzyme, and immunological cross-reaction of two subunits of the enzyme with antibodies against subunits I and II, and the holoenzyme, of Paracoccus denitrificans aa3-type cytochrome oxidase. The data presented are the first comprehensive evidence for the occurrence of aa3-type cytochrome oxidase in the plasma membrane of a cyanobacterium similar to the corresponding mitochondrial enzyme (EC 1.9.3.1).
 ...
PMID:Characterization of the cytochrome c oxidase in isolated and purified plasma membranes from the cyanobacterium Anacystis nidulans. 254 45


1 2 3 4 5 6 Next >>