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)

Biochemical composition of middle ear effusions (MEE) and serum was compared both in experimentally induced middle ear inflammation in squirrel monkeys and in otitis media in humans. The MEE and serum protein concentrations were similar in the animal experiments. In human MEE the total protein concentration of both serous and mucoid effusions was higher than the proteins of the serum. High concentrations of potassium and lower concentrations of glucose in human MEE than in serum were also observed. Activities of various oxidative (lactate dehydrogenase, malate dehydrogenase) and hydrolytic (leucine aminopeptidase, alkaline and acid phosphatase, and lysozyme) enzymes in MEE and serum were compared. The ratio of enzyme activity between MEE and serum (MEE/Serum) was greater than one in all enzymes studied. Mucoid MEE had higher activity of enzymes than serous effusions in general. Lactate dehydrogenase isoenzyme patterns were compared on electropherogram. Isoenzyme fractions 1 and 2 were each smaller in MEE than in serum whereas 4 and 5 had a significantly higher activity in MEE than in serum. Higher activities of enzymes in MEE as compared with serum are consistent with the hypothesis that MEE results from inflammatory processes occurring in the middle ear cavity. The enzymes of MEE seem to have multiple origins, namely, 1) enzymes normally present in blood, 2) enzymes from the inflamed middle ear mucosa, and 3) enzymes from leucocytes present in effusions.
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PMID:Biochemical characteristics of middle ear effusions. 81 35

Formation of opaque deposits on the anterior (air) surface of hydrophilic soft contact lenses is a problem worthy of investigation by all concerned. These deposits have been analyzed for biomaterials by chemical, biochemical, electrophoretic, and immunological techniques. Qualitative and quantitative chemical colorimetric tests revealed the presence of variable amounts of protein (5-10 microgram/lens), carbohydrate (1.0-1.2 microgram/lens), and phospholipids (0.01-0.05 micronmole/lens). Cholesterol and glucose were not present at detectable levels. Fluorescent antibody tests with appropriate controls gave positive tests for albumin, lysozyme, gamma-G-globulin, and alpha1-lipoprotein in the deposits, all proteins present in tear fluid. Deposits were most effectively removed from the lenses by the combination of heat, sodium dodecyl sulfate (SDS) detergent, and the thiol reagent dithiothreitol (DTT). SDS-denatured protein migrated on polyacrylamide gels with electrophoretic patterns corresponding to molecular weights for those proteins detected by the above antibody tests. The nature of the bonding interactions of biomaterials to the lenses was probed by chemical reagents used to remove them, employed singly and in all possible combinations. Urea, guanidine hydrochloride, potassium thiocyanate, potassium perchlorate, hydroxylamine, and EDTA were much less effective than SDS and DTT. These data suggest that apolar interactions plus disulfide bonds may be important in stabilizing the deposit structure, and point to improved cleaning procedures.
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PMID:Analysis of biomaterials deposited on soft contact lenses. 87 44

A description is given of an outbreak of equine infectious anaemia (E.I.A.) in Campania [at Naples and Aversa (Caserta)]; it was diagnosed by clinical, pathological and serological examinations (Coggins test). Using the serum of 45 horses with E.I.A. and 11 healthy horses (controls), numerous investigations were carried out on: enzymes, intrinsic coagulation factors, lipids and other substances. The results obtained were very interesting and show that in this disease there are significant increases in many enzymes (LDH, LAP, gamma-GT, CPK, PK and ALD) and copper. Insignificant increases were found in other enzymes (SDH, GLDH, MDH, ICDH, AIP, lysozyme, cholinesterase, GOT and GPT) and also intrinsic coagulation factors, lipid substances (total cholesterol, esterified cholesterol, triglycerides) and glucose. LDH-1-isoenzyme remains unchanged, whilst AcP decreases slightly.
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PMID:Biochemical studies on equine infectious anaemia. 101 May 2

Partially purified cellulase and a cellulase-containing polygalacturonase but notlysozyme extensively degraded the walls of Chlamydomonas reinhardtii and Ulothrix fimbrata and converted intact cells of the algae to spheroplasts. A streptomycete cellulase cochromatographed with the enzyme system releasing glucose from walls of these organisms, and this preparation also converted the algal cells to spheroplasts. The dominant constituent in the walls was carbohydrate, and glucose and small quantities of galacturonic acid but no amino sugars were present in acid hydrolysates of the walls. Glucose accounted for essentially all of the material solobilized by the cellulase preparation. Lysozyme acted on Cylindrospermum sp. walls, and it, but not the otherenzymes, converted some of the Cylindrospermum sp. cells to spheroplasts. Streptomycete enzymes lysing Micrococcus lysodeikticus cochromatographed with the proteins releasing reducing sugars from Cylindrospermum sp. walls, and components in the active fraction converted cells of this alga into spheroplasts. X-ray diffraction revealed that the walls of C. reinhardtii and U. fimbrata but not those of Cylindrospermum sp. contained cellulose. The data suggest that the susceptibility of the first twospecies to microbial degradation in natural ecosystems results from an attack on the cellulose in their walls, and the susceptibility of the third is linked with the microbial production of a lysozyme.
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PMID:Basis for the susceptibility of several algae to microbial decomposition. 112 56

A common antigen (KUNIN) purification method is described. The preparation obtained was highly antigenic, as proved by hemagglutination and its inhibition, and immunogenic in rabbits. Chemical analysis demonstrated the presence of an L-phosphoglycerid of the cephalin type, of protein, glucosamine, acetyl and glucose. The antigen had the character of an acidic polymer. It readily forms salt linkages with lysozyme. Phospholipase A induced the release of myristic, palmitic and stearic acids. It also destroyed both the antigenicity and immunogenicity of common antigen.
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PMID:Immunochemical studies on purified common enterobacterial antigen (KUNIN). 122 76

The crystal structure of the complex between neuraminidase from influenza virus (subtype N9 and isolated from an avian source) and the antigen-binding fragment (Fab) of monoclonal antibody NC41 has been refined by both least-squares and simulated annealing methods to an R-factor of 0.191 using 31,846 diffraction data in the resolution range 8.0 to 2.5 A. The resulting model has a root-mean-square deviation from ideal bond-length of 0.016 A. One fourth of the tetrameric complex comprises the crystallographic model, which has 6577 non-hydrogen atoms and consists of 389 protein residues and eight carbohydrate residues in the neuraminidase, 214 residues in the Fab light chain, and 221 residues in the heavy chain. One putative Ca ion buried in the neuraminidase, and 73 water molecules, are also included. A remarkable shape complementarity exists between the interacting surfaces of the antigen and the antibody, although the packing density of atoms at the interface is somewhat looser than in the interior of a protein. Similarly, there is a high degree of chemical complementarity between the antigen and antibody, mediated by one buried salt-link, two solvated salt-links and 12 hydrogen bonds. The antibody-binding site on neuraminidase is discontinuous and comprises five chain segments and 19 residues in contact, whilst 33 neuraminidase residues in eight segments have 899 A2 of surface area buried by the interaction (to a 1.7 A probe), including two hexose units. Seventeen residues in NC41 Fab lying in five of the six complementarity determining regions (CDRs) make contact with the neuraminidase and 36 antibody residues in seven segments have 916 A2 of buried surface area. The interface is more extensive than those of the three lysozyme-Fab complexes whose crystal structures have been determined, as judged by buried surface area and numbers of contact residues. There are only small differences (less than 1.5 A) between the complexed and uncomplexed neuraminidase structures and, at this resolution and accuracy, those differences are not unequivocal. The main-chain conformations of five of the CDRs follow the predicted canonical structures. The interface between the variable domains of the light and heavy chains is not as extensive as in other Fabs, due to less CDR-CDR interaction in NC41. The first CDR on the NC41 Fab light chain is positioned so that it could sterically hinder the approach of small as well as large substrates to the neuraminidase active-site pocket, suggesting a possible mechanism for the observed inhibition of enzyme activity by the antibody.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex. 138 57

Streptomyces antibioticus ETHZ 7451 formed spores in cultures grown in a liquid medium from either a spore or a mycelium inoculum. The spores formed were similar to those formed on surface-grown cultures, except for reduced heat resistance. Both types of spores were sensitive to lysozyme, which is unusual for Streptomyces spores. Glucose and other carbon sources, which promoted different growth rates, did not affect sporulation efficiency. Nitrogen sources, such as casamino acids, that allowed high growth rates suppressed the sporulation. A remarkable repression was also observed in media with some nitrogen sources that promoted noticeably lower growth rates. In permissive media, with nitrogen sources that permitted relatively high growth rates, sporulation was conditioned to the consumption of ammonium in the medium, but not to that of other nitrogen sources, such as asparagine. Phosphate did not show a repressive effect on sporulation in the assayed conditions.
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PMID:Sporulation of Streptomyces antibioticus ETHZ 7451 in submerged culture. 145 69

Nonenzymatic glycation has been found to increase in a variety of proteins in diabetic patients. The present study examined a possibility of preventing glycation and subsequent structural modifications of proteins by alpha-lipoic acid (thioctic acid) as lipoate, a substance which has gained attention as a potential therapeutic agent for diabetes-induced complications. Incubation of bovine serum albumin (BSA) at 2 mg/ml with glucose (500 mM) in a sterile condition at 37 degrees C for seven days caused glycation and structural modifications of BSA observed by SDS-PAGE, near UV absorption, tryptophan and nontryptophan fluorescence, and fluorescence of an extrinsic probe, TNS (6-(p-toluidinyl)naphthalene-2-sulfonate). When BSA and glucose were incubated in the presence of lipoate (20 mM), glycation and structural modifications of BSA were significantly prevented. Glycation and inactivation of lysozyme were also prevented by lipoate. These results suggest a potential for the therapeutic use of lipoic acid against diabetes-induced complications.
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PMID:Lipoate prevents glucose-induced protein modifications. 145 92

To study the regulation of lipogenesis in adipose tissue by insulin and growth hormone during lactation, tissue was biopsied from primiparous bovines at 30 days antepartum and 60 days postpartum. Tissue was cultured for 24 hr or 48 hr in M199 with acetate and glucose, with a change of medium at 24 hr. The three in vitro treatments were: insulin and hydrocortisone at 10 and 50 ng/ml, respectively (IH); IH + 10 ng/ml of growth hormone (G10); and IH + 100 ng/ml of growth hormone (G100). IH allowed lipogenesis rates from 50% to 85% of those in fresh tissue. Addition of 10 ng/ml of growth hormone reduced (P less than 0.05) lipogenesis; at 100 ng/ml, the effect was only slightly greater. The hypothesis that insulin and growth hormone could be degraded by bovine adipose tissue was tested. Adipose tissue cell-free extracts degraded 125I-labeled insulin, but did not degrade labeled growth hormone. The insulin protease activity was further characterized and had a pH optimum of 7.1, a maximum hydrolysis of approximately 70%, and a hydrated molecular mass of approximately 23,000 daltons. Insulin proteolysis was inhibited by specific insulin protease inhibitors and stimulated by disulfide reducing agents. Bovine growth hormone, prolactin, and histone inhibited (P less than 0.05) the proteolysis of insulin, while bovine serum albumin, egg albumin, trypsin inhibitor, and lysozyme did not. Adipose tissue from pregnant and lactating bovines was sensitive to insulin and growth hormone, and growth hormone may modulate activity of an insulin-specific protease.
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PMID:Growth hormone alters metabolic effects and proteolysis of insulin in adipose tissue during lactation. 157 Mar 58

The combined effect of the salivary peroxidase system and lysozyme on the glucose uptake of Streptococcus mutans NCTC 10449 was investigated. The bacteria were grown to late-exponential phase, washed, re-suspended in buffer at pH6, and incubated with (1) 50 micrograms/mL lysozyme from human milk for 60 min; (2) 7-15 mumol/L hypothiocyanous acid/hypothiocyanite for 10 min; and (3) lysozyme for 60 min prior to addition of and incubation with hypothiocyanous acid/hypothiocyanite for 10 min. Glucose uptake was initiated by adding the bacterial suspensions to 10 mL of pre-warmed 50 mumol/L glucose containing 0.98 mumol/L D-(U-14C-)-glucose, and the mixture was incubated in a shaking water-bath at 37 degrees C. Samples were withdrawn at various time intervals, rapidly filtered through 0.45-microns membranes, washed with ice-chilled buffer, and the incorporated radioactivity determined. Lysozyme stimulated S. mutans glucose uptake slightly, but significantly inhibited S. rattus glucose metabolism. A 20-30% inhibition of radiolabeled glucose incorporation was observed with hypothiocyanous acid/hypothiocyanite alone. Incubation of the bacteria with lysozyme prior to addition of hypothiocyanous acid/hypothiocyanite containing peroxidase resulted in a total inhibition of the glucose uptake. In contrast, lysozyme in combination with hypothiocyanous acid/hypothiocyanite without peroxidase gave only a 30-50% inhibition. The addition of 5 mmol/L dithiothreitol after incubation with lysozyme and hypothiocyanous acid/hypothiocyanite eliminated the inhibition of the bacterial glucose uptake. The viability of S. mutans was not affected by treatment with any of the components used. Our results indicate that physiological concentrations of lysozyme and the salivary peroxidase system components have a synergistic effect which results in a significant inhibition of glucose metabolism by S. mutans.
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PMID:Lysozyme enhances the inhibitory effects of the peroxidase system on glucose metabolism of Streptococcus mutans. 157 81


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