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)

Biocompatibility is redefined as the quality of being mutually tolerant with life. In so far as this represents a quality which is as likely to be achieved as is the alchemist's dream of turning lead into gold, a compromise approach is recommended. It is suggested that all extracorporeal or body invasive procedures stimulate the inflammatory defence mechanism of the body by stimulating the monocyte to produce a family of polypeptides currently known collectively as Interleukin-1 (IL-1). So far two dissimilar gene products have been cloned and there are probably more. The IL-1 group of polypeptides possess hormonal functions which orchestrate nearly every instrument of the body's defence system. Inducers of IL-1 are present in dialysate and induce bacterial pyrogen and acetate. In addition bacterial cell wall glycoprotein may be cleaved into muramyl peptides by the release of granulocyte lysozyme at the membrane interface. Muramyl dipeptides have been found in CAPD drain fluid and are more potent inducers of IL-1 than endotoxin. Membrane activation of the fifth component of the complement with the release of C5a will also induce monocytes to produce IL-1. The consequences of repeated stimulation of the acute phase response are undesirable and may include muscle wasting, osteopenia and bone cysts (Shrinking man syndrome), fibrosis of scapulo-humeral joints and the carpal-tunnel syndrome. These latter lesions are often associated with deposition of amyloid fibrils related to beta 2-microglobulin. Efforts to reduce these complications are urgently required.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The relationship between biocompatibility and interleukin-1. 350 5

Thirty-eight production workers exposed to Ni and 35 exposed to Co were examined for the content of Ni and Co in hair, the serum concentration levels of immunoglobulins, IgG, IgA, IgM, and IgE, and serum proteins, alpha 2-macroglobulin (A2M), transferrin (TRF), alpha 1-antitrypsin (A1AT), ceruloplasmin (CPL), lysozyme (LYS), and alpha 1-glycoprotein (A1GP). Atomic absorption analysis of hair revealed that the respective geometric mean values of Ni and Co in Ni-exposed workers were 216.75 and 3.31 micrograms X g-1 and in Co-exposed workers 34.5 and 96.81 micrograms X g-1. These values were significantly higher than respective control values found in nonexposed individuals matched by age (Ni: 3.31 and Co: 0.38 micrograms X g-1). These findings suggest that hair analysis is a suitable method for the biological monitoring of exposure to these two metals. Tests for serum proteins revealed that nickel workers differed from controls by exhibiting significantly elevated IgG, IgA, and IgM levels; cobalt workers by a significant elevation of IgA level; and both exposed groups by a significant drop in the IgE level. A significant rise in the concentration (P less than 0.001-P less than 0.005) was also recorded in the case of A1AT, A2M, CPL, and LYS. The possible biomedical implications of these immunobiochemical findings are critically analyzed.
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PMID:Human exposure to nickel and cobalt: biological monitoring and immunobiochemical response. 373 11

Fibrin and hyaluronic acid (HA) are macromolecules whose concentrations are elevated at the same time in the extracellular space of damaged tissues. We have investigated whether HA can bind to fibrinogen using solid phase and soluble assays. Purified human fibrinogen specifically bound to HA-Sepharose to a greater extent (greater than 5-fold) than did alpha 1-acid glycoprotein, DNaseI, ovalbumin, haptoglobin, or lysozyme. Fibrinogen did not bind to ethanolamine-Sepharose, a control chromatographic support. Treatment of HA-Sepharose containing bound 125I-fibrinogen with ovine testicular hyaluronidase released 44% of the 125I radioactivity, indicating that fibrinogen was specifically bound to HA. Moreover, 125I-fibrinogen bound to HA-Sepharose could be displaced by free HA but not by either of the monosaccharide components of this polymer, glucuronic acid, or N-acetylglucosamine. Chondroitin sulfate and polygalacturonic acid competed only weakly for bound 125I-fibrinogen. Bound 125I-fibrinogen was also not released by high concentrations of NaCl (up to 4 M), indicating that the interaction is not simply ionic. The apparent affinity of fibrinogen for HA covaried with the molecular weight of the HA. Small HA oligosaccharides (Mr = 3900) were only 50% as effective as larger HA (Mr = 8 X 10(5)) in eluting bound 125I-fibrinogen from HA-Sepharose. The optimal oligosaccharide size for displacement of bound 125I-fibrinogen was greater than or equal to 200 monosaccharides. Additionally, the amount of 125I-fibrinogen bound to HA-Sepharose was directly related to the size of the HA-amine linked to the affinity support. The affinity constant for fibrinogen binding to 125I-HA (approximately 150 monosaccharides) is estimated to be at least 2 X 10(7) M-1. These results demonstrate for the first time a specific, reversible binding between HA and fibrinogen.
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PMID:Human fibrinogen specifically binds hyaluronic acid. 374 4

Elimination of low molecular weight proteins during sequential ultrafiltration/dialysis was studied in 29 uremic patients. Beta-2-microglobulin, retinol binding protein, free light chains lambda and kappa, Zn-alpha-2-glycoprotein, hemopexin, prealbumin, hemoglobin, albumin, acid alpha-1-glycoprotein, haptoglobin, alpha-1-antichymotrypsin, ribonuclease, lysozyme, amylase, non-specific esterase, and proteolytic activity were detected in all ultrafiltrates tested. The level of total protein and ribonuclease was determined in 36 crude ultrafiltrates from 23 patients. Concentrated ultrafiltrates were used to quantitate retinol binding protein, prealbumin, albumin, lysozyme, and amylase. Other proteins identified in the ultrafiltrates are present in trace amounts. The question was discussed whether ++inextensive but systematic loss of proteins during hemofiltration in chronic RDT might be the cause of patient homeostasis disturbances.
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PMID:Detection of plasma proteins during sequential ultrafiltration/dialysis. 406 85

1. The purification of wheat-germ agglutinin from commercial wheat germ is described. By ion-exchange chromatography three active proteins (isolectins) were separated, one of which was examined in detail. 2. The amino acid composition is unusual, as 20% of residues are half-cystine and 21% are glycine. Unlike most lectins and contrary to previous reports, this protein is not a glycoprotein. 3. The efficiency of various saccharides as inhibitors of the agglutination reaction was investigated and from this the specificity of the binding site was inferred. Of monosaccharides, only derivatives of glucose with a 2-acetamido group and a free 3-hydroxyl group are effective inhibitors, and glycosides of either anomeric configuration are bound. Oligosaccharides are much more powerful inhibitors of agglutination than are monosaccharides. 4. It is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that proposed for hen's-egg-white lysozyme.
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PMID:The purification, composition and specificity of wheat-germ agglutinin. 473 92

Cervical mucus collected from 32 women on Cycle Days 10-20 was subjected to agarose gel electrophoresis, liquid film electrophoresis, and Sepharose 6B chromatography. To prepare the material, pooled mucus was reduced with mercaptoethanol, centrifuged at 3000 rpm for 20 minutes, dialyzed against distilled water, and lyophilized. After 1 hour at 3 volts/cm, agarose gel electrophoresis revealed a single band of protein stained by amidoschwartz. Immunologic methods demonstrated serum albumin, lactoferin, IgA-globulins and alpha2-globulins. Periodic acid and Schiff reagent showed a glycoprotein band superimposed over the protein. Toluidine blue stain for acid glycoproteins revealed slow and rapid components. Preparative liquid film electrophoresis separated mucleic acids (260 m mcm), sulfomucins, sialomucins, and sialic acid, a small slow peak of sialomucins and lysozyme as well as several serum proteins. Gel filtration on Sepharose 2B distinguished a minor peak of high molecular weight (over 1 million), sialomucins, a major component (300,000-500,000 molecular weight) identified as sialomucins free of protein, and a third low molecular weight, heterogeneous fraction corresponding to mucus proteins, plasma glycoproteins, mucus glycoproteins, and cervical sulfomucins.
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PMID:[The characteristics of the cervical mucins in the ovulatory phase]. 535 72

Human and canine airway mucosa in vitro synthesizes and secretes mucus glycoprotein, proteoglycans and lipids which can be separated by density gradient ultracentrifugation in caesium bromide. In secretions from unstimulated explants, the small amount of mucus glycoprotein present is found in association with proteoglycans. 'Free' mucus glycoprotein of typical buoyant density is present only after stimulation of submucosal gland secretion by methacholine. Lipids are synthesized, at least in part, by the airway mucosa and occur in explant secretions as a viscoelastic gel, suggesting that they significantly influence the rheological properties of airway mucus. In addition to cholinergic and adrenergic secretomotor neurons, the airway mucosa is innervated by peptidergic fibres containing immunoreactivity to vasoactive intestinal peptide (VIP) and substance P (SP). In explants of non-bronchitic human airway, VIP inhibits baseline glycoprotein and lysozyme secretion; in canine airway mucosa, by contrast, VIP is a weak partial secretory agonist. SP is the most potent agonist of canine airway glycoprotein release described to date and appears to evoke secretion by a direct action on a stereospecific SP receptor rather than by inducing release of other endogenous secretagogues. VIP and SP have little effect on glycoprotein discharge by mucous and serous cells of the submucosal gland; SP appears to induce secretion by causing contraction of submucosal gland ducts. This may represent the most rapid way for delivering mucus into the airway in response to injury or irritation of airway epithelium.
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PMID:Airway mucus: composition and regulation of its secretion by neuropeptides in vitro. 608 50

In vitro studies of the behaviour of the trypanosomatid flagellates Trypanosoma brucei and Leishmania hertigi in the presence of cell-free haemolymph of locusts, Schistocerca gregaria and cockroaches, Periplaneta americana revealed the presence of parasite agglutinins. The range of normal values of agglutination titres was 2(-4) to 2(-13). Physico-chemical treatment of haemolymph indicated that these agglutinins are protein or glycoprotein in nature and are only partially affected by heat treatment below 65 degrees C, at which temperature incubation of haemolymph for 30 min abrogated all agglutination. Agglutination was not dependent on the presence of Ca2+ or Mg2+. Prior injection of locusts and cockroaches with T. brucei and L. hertigi significantly increased agglutinin titres between Days 4 and 6 in cockroaches (P less than 0.05) and from Days 2 to 4 when L. hertigi was inoculated into locusts. The induced differences in titres observed in locusts infected with T. brucei were not significant. Lysozyme levels were significantly increased after inoculation of T. brucei into cockroaches compared with placebo-inoculated and uninoculated controls. L. hertigi inoculation produced significant increases in lysozyme levels compared with controls between Days 1 and 7 in locusts and 3 to 6 in cockroaches. These studies indicate that, at least in easily manipulated model systems, induced responses to intrahaemocoelic inoculation to trypanosomes and Leishmania can occur. As far as we are aware this is the first report of an induced response of an insect to such important parasites. The possibility that induced responses in natural vector to this parasites occurs requires investigation.
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PMID:Naturally occurring agglutinins against trypanosomatid flagellates in the haemolymph of insects. 609 91

An enzyme was identified in human serum which unlike lysozyme cleaved the amide bond between N-acetyl-muramic acid and L-alanine of the peptide side chain of the rigid layer (murein) of Escherichia coli. The N-acetyl-muramyl-L-alanine amidase released all of the peptide side chains including those to which the lipoprotein is bound. A portion of the peptide side chains of the Micrococcus lysodeikticus murein was also hydrolysed from the polysaccharide chains. E. coli, M. lysodeikticus, Bacillus subtilis and Staphylococcus aureus were not killed by the amidase. Treatment of E. coli with EDTA or osmotic shock rendered the cells sensitive to the amidase and they were killed. Possible biological functions of the amidase are discussed. The enzyme was separated from lysozyme in human serum. Gel permeation chromatography indicated a molecular weight of the active enzyme of 82,000 while gel electrophoresis in the presence of sodium dodecyl sulfate revealed a molecular weight of 75,000. Thus, the enzyme probably consists of a single polypeptide chain. Incubation with neuraminidase rendered the amidase more basic suggesting the release of sialic acid residues. The modified glycoprotein disclosed an increased activity to murein. Enzyme activity was inhibited by p-chloromercuribenzene sulfonate and ethyleneglycol-bis(2-aminomethyl) tetraacetate (EGTA) at 1 and 0.2 mM concentration, respectively, whereas EDTA up to 5 mM was without effect. The amidase was also inactivated by agents that reduce disulfide bridges.
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PMID:Murein hydrolase (N-acetyl-muramyl-L-alanine amidase) in human serum. 615 47

In the present investigation 11 females of normal constitution were subjected to a standardized fasting diet for 8 days. Three subjects dropped out early during the experimental period. Saliva and blood samples were collected before, during and after the fasting period. Serum analyses were made of some parameters often studied during undernutrition. As expected, values for creatinine and uric acid were increased. Secretion rate, pH, buffer capacity, electrolytes, total protein, carbohydrates, some antibacterial substances, the amount of Streptococcus mutans, total streptococci, and lactobacilli were determined in the saliva samples. The rate of plaque formation was also estimated. The effect of fasting on the measured parameters varied greatly among the individuals. Fasting caused a significant decrease in secretion rate, concentration of phosphate and sialic acid in stimulated whole saliva. There was no significant increase in concentration of any substance measured. The decrease of the ratio of sialic acid to protein indicates a disturbance of glycoprotein synthesis. In resting saliva the activity of a bacteria-aggregating glycoprotein appeared to be unchanged, whereas the decreases in thiocyanate concentration and lysozyme activity were statistically significant. Lactoperoxidase activities did not change significantly. The amount of IgA, IgG, IgM as well as the microbial counts showed no changes. The rate of plaque formation increased during fasting.
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PMID:Studies of the effect of diet on saliva secretion and caries development: the effect of fasting on saliva composition of female subjects. 620 45


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