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

---

Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A complex comparative study of the characteristics of nonspecific resistance in different species of laboratory animals immunized with vaccine STI against anthrax has revealed the existence of marked interspecific differences between noninbred white mice, guinea pigs, rabbits and noninbred white rats in such characteristics as phagocytic activity, oxygen-dependent function of polymorphonuclear blood leukocytes, serum beta-lysin and lysozyme.
...
PMID:[The nonspecific resistance indices of different species of laboratory animals immunized with STI anthrax vaccine]. 805 81

LL-H, a virulent phage of Lactobacillus delbrueckii subsp. lactis, produces a peptidoglycan-degrading enzyme, Mur, that is effective on L. delbrueckii, Lactobacillus acidophilus, Lactobacillus helveticus, and Pediococcus damnosus cell walls. In this study, the LL-H gene mur was cloned into Escherichia coli, its nucleotide sequence was determined, and the enzyme produced in E. coli was purified and biochemically characterized. Mur was purified 112-fold by means of ammonium sulfate precipitation and cation-exchange chromatography. The cell wall-hydrolyzing activity was found to be associated with a 34-kDa protein. The C-terminal domain of Mur is not essential for catalytic activity since it can be removed without destroying the lytic activity. The N-terminal sequence of the purified lysin was identical to that deduced from the nucleotide sequence, but the first methionine is absent from the mature protein. The N-terminal part of this 297-amino-acid protein had homology with several Chalaropsis-type lysozymes. Reduction of purified and Mur-digested L. delbrueckii cell wall material with labeled NaB3H4 indicated that the enzyme is a muramidase. The temperature optimum of purified Mur is between 30 and 40 degrees C, and the pH optimum is around 5.0. The LL-H lysin Mur is stable at temperatures below 60 degrees C.
...
PMID:Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin. 852 15

Fluorescent properties of indo-1 in protein containing solutions have been investigated. No changes have been defined in indo-1 fluorescent parameters in solutions of such proteins as trypsin, calmodulin, papain, lysozyme. Significant changes of indo-1 fluorescent parameters have been observed in solutions of histones, bovine and human serum albumins. Results obtained suggest that indo-1 binds well with protein sites containing hydrophobic "pockets" and positively charged amino-acid residues such as arginine and lysin. The destruction of the compact structure of serum albumin in 8 M urea leads to shift of indo-1 fluorescence spectrum and it approaches to the spectrum in water. Fluorescence spectra of indo-1 in dioxane prove that the binding of indo-1 by some proteins occurs in hydrophobic microenvironment of protein globule.
...
PMID:[Effect of medium polarity and protein microenvironment on indo-1 fluorescence]. 859 74

The lysis genes of a Lactobacillus phage phi g1e were cloned, sequenced, and expressed in Escherichia coli. Nucleotide sequencing of a 3813-bp phi g1e DNA revealed five successive open reading frames (ORF), Rorf50, Rorf118, hol, and lys and Rorf175, in the same DNA strand. By comparative analysis of the DNA sequence, the putative hol product (holin) has an estimated molecular weight is 14.2 kDa, and contains two potential transmembrane helices and highly charged N- and C-termini, resembling predicted holins (which are thought to be a cytoplasmic membrane-disrupting protein) encoded by other phages such as mv1 from Lactobacillus bulgaricus, phi adh from Lactobacillus gasseri, as well as monocins from Listeria. On the other hand, the putative phi g1e lys product (lysin) of 48.4 kDa shows significant similarity with presumed muramidase, known as a cell wall peptidoglycandegrading enzyme, encoded by the Lactobacillus phage mv1 and phi adh, the Lactococcus lactis phage phi LC3, and the Streptococcus pneumoniae phages Cp-1, Cp-7 and Cp-9. When expressed in E. coli, the phi g1e lysin and/or holin decreased the cell turbidity significantly, suggesting that the phi g1e hol-lys system is involved in cytolytic process.
...
PMID:Cloning, sequence analysis, and expression of the genes encoding lytic functions of Bacteriophage phi g1e. 891 56

Leukocytes use an array of antimicrobial peptides and proteins to help them destroy invading microorganisms. These endogenous antibiotic molecules are remarkable for their structural variety, rapid evolutionary divergence, intraspecies variation, and complex yet subtle interactions with their targets. This arsenal has been studied most extensively in neutrophils, where its members include lactoferrin, secretory phospholipase A2, lysozyme, and the cathelicidins in the secretory granule compartment; defensins, bactericidal permeability inducing protein, serprocidins, and (again) lysozyme in the azurophil granule compartment; and calprotectin in the cytosolic compartment. That antimicrobial peptides and proteins are not limited to neutrophils and other phagocytes was made clear by the recent discovery of a microbicidal protein, NK lysin, in porcine natural killer cells and cytotoxic T lymphocytes. The structural homology of NK-lysin to amebapore, an antimicrobial cytolytic peptide of the parasitic protozoan Entamoeba histolytica, provides remarkable support for a long-suspected evolutionary connection between the leukocytes of higher animals and their unicellular, protozoan ancestors.
...
PMID:Antimicrobial peptides of leukocytes. 905 Mar 80

The two lysis genes cph1 and cpl1 of the Streptococcus pneumoniae bacteriophage Cp-1 coding for holin and lysozyme, respectively, have been cloned and expressed in Escherichia coli. Synthesis of the Cph1 holin resulted in bacterial cell death but not lysis. The cph1 gene was able to complement a lambda Sam mutation in the nonsuppressing E. coli HB101 strain to produce phage progeny, suggesting that the holins encoded by both phage genes have analogous functions and that the pneumococcal holin induces a nonspecific lesion in the cytoplasmic membrane. Concomitant expression of both holin and lysin of Cp-1 in E. coli resulted in cell lysis, apparently due to the ability of the Cpl1 lysozyme to hydrolyze the peptidoglycan layer of this bacterium. The functional analysis of the cph1 and cpl1 genes cloned in a pneumococcal mutant with a complete deletion of the lytA gene, which codes for the S. pneumoniae main autolysin, provided the first direct evidence that, in this gram-positive-bacterium system, the Cpl1 endolysin is released to its murein substrate through the activity of the Cph1 holin. Demonstration of holin function was achieved by proving the release of pneumolysin to the periplasmic fraction, which strongly suggested that the holin produces a lesion in the pneumococcal membrane.
...
PMID:Functional analysis of the two-gene lysis system of the pneumococcal phage Cp-1 in homologous and heterologous host cells. 944 May 7

The low doses of gamma-irradiation activate the factors of nonspecific protection of the poultry organisms. There is the rise of antimicrobial characteristics of skin and mucous membrane of oral cavity of bactericide ability of blood serum due to increased content of lysozyme, beta-lysin and number of normal antibodies in it. Gamma-irradiation promotes the formation of a stronger immunity and a favourable outcome of an infectious process.
...
PMID:[Immunological aspects of the effects of low-dose gamma irradiation: nonspecific factors of protection and immunological reactivity of poultry]. 946 38

The nucleotide sequence of a DNA fragment previously shown to contain the attachment site (attP) of Oenococcus oeni phage fOg44 (. Arch. Virol. 143, 523-536) has been determined. Sequence analysis indicated that this 6226bp EcoRI fragment harbours an integrase gene, in the vicinity of a direct repeat rich region defining attP, as well as genes encoding a muramidase-related lysin (Lys) and a holin polypeptide (Hol). Transcriptional studies suggested that lys and hol are mainly co-expressed, late in the lytic cycle, from a promotor located upstream of lys. Between the lytic cassette and the phage integration elements three additional open reading frames were found: orf217 and orf252 of unknown function and orf72, the putative product of which bears 32% identity with acidic excisionases from other Gram positive phages. We have established that the first two orfs, as well as the predicted promotor of orf72, are included in a 2143-bp DNA segment missing from the genome of the deletion mutant fOg44Delta2. Although lysogens of fOg44 and fOg44Delta2 exhibited similar properties, each phage produced two distinguishable types of lysogenic strains, differing in inducibility and immunity to other oenophages.
...
PMID:Gene organization in a central DNA fragment of Oenococcus oeni bacteriophage fOg44 encoding lytic, integrative and non-essential functions. 988 28

Lysis of trypsinized Group A streptococcal cell walls with phage-associated lysin releases into solution dialyzable and non-dialyzable mucopeptide fractions composed of N-acetylglucosamine, N-acetylmuramic acid and alanine, glutamic acid, lysine, and glycine in addition to the characteristic group-specific carbohydrate. The latter substance contains appreciable amounts of N-acetylmuramic acid and the amino acids as well as N-acetylglucosamine and rhamnose. Hot formamide extraction of the cell walls results in a soluble fraction of group-specific carbohydrate and an insoluble residue. The Group A carbohydrate in this instance is composed of rhamnose and N-acetylglucosamine. The composition of the insoluble residue is similar to that of the mucopeptide fractions released from the cell wall by phage-associated lysin. This residue was shown by electron microscopy to be composed of discrete discs which appear similar in structure to the intact cell wall. The specific carbohydrate obtained by hot formamide extraction of Group A-variant cell walls was composed almost exclusively of rhamnose. The residue fraction was similar to that of Group A. The residue of cell walls extracted with hot formamide is extensively solubilized not only by phage-associated lysin and S. albus enzyme, but also by lysozyme, which has no measurable effect on the intact streptococcal cell wall.
...
PMID:Studies on the chemical structure of the streptococcal cell wall. I. The identification of a mucopeptide in the cell walls of groups A and A-variant streptococci. 1375 97

The trypsinized cell walls of Group C streptococci contain two components, the group-specific carbohydrate and a mucopeptide polymer. Hot formamide extraction of Group C cell walls results in a soluble group-specific carbohydrate fraction and an insoluble mucopeptide residue. This mucopeptide, similar in composition to that of Groups A and A-variant streptococci, contains N-acetylglucosamine, N-acetylmuramic acid, alanine, glutamic acid, lysine, and glycine. It is dissolved by the muralytic enzymes, including lysozyme, which does not attack the whole cell wall. Lysis of the cell wall by phage-associated lysin results in the release of soluble fragments composed of the elements of mucopeptide. Group C carbohydrate extracted with formamide is composed primarily of N-acetylgalactosamine and rhamnose. Serological studies suggest that the specificity of Group C carbohydrate is determined by the N-acetylgalactosamine.
...
PMID:Studies on the chemical structure of the streptococcal cell wall. II. The composition of group C cell walls and chemical basis for serologic specificity of the carbohydrate moiety. 1445 33


<< Previous 1 2 3 4 5 6 7 Next >>

---