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)

A plastic intraoral (IO) cup developed to facilitate collection of human parotid saliva was tested on two groups of patients. Samples collected in both IO and tubed cups exhibited no significant differences in lysozyme or lactoperoxidase activity, levels of total protein or secretory IgA, or in flow rates. Results suggest that the IO cup provides a simple, reliable method for collecting parotid saliva.
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PMID:A plastic intraoral device for the collection of human parotid saliva. 26 51

Human milk was subjected to heat treatments of graded severity and examined for its content of immunoglobulins, lactoferrin, lysozyme, vitamin B12-and folate-binder proteins, and lactoperoxidase. Holder pasteurization (62.5degrees C 30 minutes) reduced the IgA titer by 20%, and destroyed the small content of IgM and most of the lactoferrin. Lysozyme was stable to this treatment, but with an increase in temperature there was progressive destruction, to near 100% at 100degrees C. The same was broadly true of the capacity of milk to bind folic acid and potect it against bacterial uptake; with vitamin B12 the binder was more labile at 75degrees C than at 100degrees C. The milk contained no detectable lactoperoxidase.
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PMID:Influence of the heat treatment of human milk on some of its protective constituents. 31 82

The antimicrobial activity of various proteins and other substances in milk and colostrum is discussed. These factors include antibodies, complement, lactoferrin and transferrin, lactoperoxidase and lysozyme. The possible importance of these factors in protecting the newborn infant against infectious diseases is discussed.
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PMID:[Antimicrobial factors in milk and colostrum: their importance for the newborn infant (author's transl)]. 34 62

The bactericidal action that results from lactoperoxidase-catalyzed oxidation of iodide or thiocyanate was studied, using Escherichia coli as the test organism. The susceptibility of intact cells to bactericidal action was compared with that of cells with altered cell envelopes. Exposure to ethylenediaminetetraacetic acid, to lysozyme and ethylenediaminetetraacetic acid, or to osmotic shock were used to alter the cell envelope. Bactericidal action was greatly increased when the cells were exposed to the lactoperoxidase-peroxide-iodide system at low temperatures, low cell density, or after alteration of the cell envelope. When thiocyanate was substituted for iodide, bactericidal activity was observed only at low cell density or after osmotic shock. Low temperature and low cell density lowered the rate of destruction of peroxide by the bacteria. Therefore, competition for peroxide between the bacteria and lactoperoxidase may influence the extent of bactericidal action. Alteration of the cell envelope had only a small effect on the rate of destruction of peroxide. Instead, the increased susceptibility of these altered cells suggested that bactericidal action required permeation of a reagent through the cell envelope. In addition to altering the cell envelope, these procedures partly depleted cells of oxidizable substrates and sulfhydryl components. Adding an oxidizable substrate did not decrease the susceptibility of the altered cells. On the other hand, mild reducing agents such as sulfhydryl compounds did partly reverse bactericidal action when added after exposure of cells to the peroxidase systems. These studies indicate that alteration of the metabolism, structure, or composition of bacterial cells can greatly increase their susceptibility to peroxidase bactericidal action.
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PMID:Susceptibility of Escherichia coli to bactericidal action of lactoperoxidase, peroxide, and iodide or thiocyanate. 34 97

A simple and rapid method is described for the removal of lysozyme from human whole salivary supernatant. Saliva specimens were adsorbed with Micrococcus lysodeikticus. The saliva so treated was depleted of 95% of the lysozyme activity. Changes in total protein, lactoperoxidase, lactoferrin, immunoglobulin A, and the proportions of several anionic proteins were less than 10%. It is concluded that adsorption of saliva with M. lysodeikticus is a suitable procedure for the preparation of saliva that is selectively deficient in lysozyme.
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PMID:Simple and rapid procedure for the selective removal of lysozyme from human saliva. 52 61

Rabbit peritoneal polymorphonuclear leucocytes were induced to aggregate by a variety of bacterial species. In the absence of serum, Gram-negative bacteria were more effective at inducing aggregation than Gram-positive. The most effective micro-organism tested, Acinetobacter sp. 199A, was readily phagocytosed and also induced extracellular secretion of the granule enzymes peroxidase and lysozyme. Isolated endotoxin from this bacterial species was highly effective in inducing aggregation and granule enzyme release. Endotoxin-induced aggregation was associated with a large increase in the amount of lactoperoxidase-catalysed iodination of surface protein. Only one iodinatable protein was detected, of molecular weight 150 000. It is postulated that phagocytosis of Gram-negative bacteria, followed by granule enzyme release, accelerates the rate of membrane recycling and that this brings new adhesive protein to the surface more rapidly.
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PMID:Changes in the surface properties of rabbit polymorphonuclear leucocytes, induced by bacteria and bacterial endotoxin. 59 74

Both the immunoglobulins and non-specific antibacterial factors in milk from cows immunized with pathogenic oral bacteria have the potential to influence the oral microflora during passive immunization studies. The first six milks after calving were collected from 2 cows immunized with adjuvant and from 14 cows immunized with adjuvant and heat-killed strains of periodontopathic Actinomyces, Porphyromonas, Prevotella, and Fusobacterium. Analysis of the products from the first to the sixth milks revealed that the protein and lysozyme content decreased approximately 66 and 72%, respectively; the mean specific activity of the enzyme remained relatively constant. In contrast, the mean lactoperoxidase activity increased 2.3-fold in the second milking and increased further in the fourth and sixth milkings. The mean iron-binding activity increased 1.2-fold from the first to the second milkings and then decreased 3.6-fold through the sixth milking. Cows immunized with adjuvant alone showed similar responses. Per unit volume, the milk contained approximately 150 times less lysozyme than whole human saliva obtained from six subjects but higher concentrations of lactoperoxidase and iron-binding components. Purified bovine nonspecific factors prevented the growth of the bacteria used for immunization when bacteria were tested at concentrations similar to those found in saliva and milk. Because bovine nonspecific antibacterial factors could influence both the pathogenic target bacteria and the indigenous microflora in oral passive immunization studies with bovine immunoglobulins, the presence of these proteins should be considered.
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PMID:Nonspecific antibacterial factors in milk from cows immunized with human oral bacterial pathogens. 150 May 76

In an attempt to clarify the mechanism(s) of increased susceptibility to oral infection in diabetics, we examined the levels of salivary antibacterial factors, including lysozyme, lactoperoxidase, and lactoferrin, in diabetic hamsters whose condition was induced with streptozotocin. Saliva was collected from these hamsters periodically for 19 weeks after the administration of streptozotocin. Diabetes persisted with significant hyperglycemia throughout the experiment after a single injection of streptozotocin. There was no significant difference between groups in the amount of saliva secreted. In diabetic hamsters, lysozyme activity decreased by 56% and lactoperoxidase activity decreased by 53% compared with the control hamsters 19 weeks after the administration of streptozotocin. There was no significant difference between groups in the amount of salivary lactoferrin. However, the ratio of lactoferrin to total protein increased to approximately double the amount of that of the control hamsters. Insulin treatment had a significant effect on lysozyme and lactoperoxidase activity, recovering 73 and 74% those of the controls, respectively, and the ratio of lactoferrin to total salivary protein reverted to normal values. Growth inhibition of Lactobacillus plantarum ATCC 8014 with whole saliva and amylase activity significantly decreased in diabetic hamsters. The position of each protein band of whole saliva on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was almost the same for control and diabetic hamsters; however, there was some variability in band intensity.
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PMID:Levels of salivary lysozyme, lactoperoxidase, and lactoferrin in diabetic hamsters. 258 Jul 90

The interaction of lactoperoxidase with lysozyme and ribonuclease as well as immunoglobulins from cow milk has been investigated. As gel filtration and enzyme kinetics experiments have shown, the lactoperoxidase was slightly activated by complexing to lysozyme, while IgA and IgM were inhibitory for the peroxidase. Oh the other hand, IgG and ribonuclease had no effect on the enzyme activity although the latter did form a complex with the lactoperoxidase. The interaction between the lysozyme and lactoperoxidase appears to be rather specific since the alteration of the lactoperoxidase sugar moiety by periodate oxidation, prevented the formation of the lactoperoxidase-lysozyme complex.
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PMID:Interaction of lactoperoxidase with enzymes and immunoglobulins in bovine milk. 263 59

Binding of human lactoferrin (hLf) by purified rat liver plasma membranes was studied to clarify whether the liver possesses specific hLf receptors. The binding was rapid between 4 degrees and 37 degrees C, with a pH optimum close to 5.0. At 22 degrees C and in glycine-NaOH (5 mM, pH 7.4) containing 150 mM NaCl and 0.5% albumin, 1 microgram of membrane bound a maximum of 11.8 ng hLf. The dissociation constant of the interaction was 1.6 X 10(-7) M. Other proteins of high isoelectric points (lactoperoxidase, lysozyme, and particularly salmine sulfate) and a piperazine derivative inhibited hLf binding in a concentration-dependent manner. In contrast, monosaccharides (galactose, N-acetylgalactosamine, mannose, and fucose) were ineffective. By omitting NaCl from the incubation buffer, binding was increased 3.6-fold. Erythrocyte ghosts bound hLf less firmly and alveolar macrophages more firmly than hepatic plasma membranes. Liver cell fractionations performed after the intravenous injection of labeled hLf showed that approximately 88% of the hepatic radioligand was associated with parenchymal cells. When binding was expressed per unit of cell volume, however, more hLf was present in nonparenchymal than in parenchymal cells, implying that the above value was determined by the relative cell masses rather than affinities alone. It is concluded that the binding of hLf by hepatic plasma membranes is electrostatic, i.e., is mediated by the cationic nature of the ligand, and that it is explicable in terms of a "specific nonreceptor interaction" of the generalized type proposed by Cuatrecasas and Hollenberg (Adv. Protein Chem. 30: 251-451, 1976).
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PMID:Interaction of human lactoferrin with the rat liver. 298 44


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