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)

The outer membrane of Vibrio parahaemolyticus strain 3283-61 (serotype O2:K3) was isolated from blebs released upon spheroplast formation, in the presence of lysozyme and EDTA, by isopycnic sucrose density gradient centrifugation. SDS-PAGE of the outer membrane fraction prepared from cells grown in nutrient broth containing 3% (w/v) NaCl revealed five major proteins, designated a to e, with apparent approximate molecular weights: a, 44 000; b, 36 000; c, 33 500; d, 26 500; e, 22 000. An increase in NaCl concentration in the growth medium resulted in an increase of proteins b and c, whereas a decrease to 0.5% (w/v) induced two additional major proteins with respective molecular weights of about 35 000 and 32 000. Proteins a and b appeared to be loosely associated with the peptidoglycan layer since they were largely retained after extraction with 2% (w/v) SDS at 50 degrees C for 30 min. Proteins c and/or e may play a role in phage VP1-receptors since phage-resistant mutants derived from strain 3283-61 had significantly diminished amounts of both proteins. The major outer membrane proteins varied in number and molecular weight in strains of V. parahaemolyticus belonging to different K-serotypes.
J Gen Microbiol 1983 Oct
PMID:Isolation and characterization of the outer membrane from Vibrio parahaemolyticus. 665 59

Spores of Bacillus cereus mutants selected for slow response to germinants and sensitivity to lysozyme were found to be deficient in coat, but were heat-resistant and contained the same quantity of dipicolinic acid as the wild-type. While the average coat protein content of the spores was 25% of the wild-type, many spores were coatless with large whorls of coat deposited in the cytoplasm. These coat deposits were isolated in Renografin gradients and found to cross-react immunologically with wild-type coat. The proteins extractable from these deposits were virtually identical to those extracted from wild-type spores. The morphology of the coat deposits was very similar to coats of wild-type spores, but with a deficiency of the outermost cross-patched layer. The sites of formation and deposition were altered. Since the mutant reverted to a phenotype identical to the parental strain with a frequency consistent with an initial point mutation, apparently a single defect resulted in alteration of the deposition of the spore coats on to the outer forespore membrane. Despite this defect, mutant cells were able to synthesize and process spore coat precursors into an array of morphological layers very similar to the wild-type. There are apparently distinct morphogenetic pathways for the formation of the spore body and coat layers.
J Gen Microbiol 1980 Jan
PMID:A Bacillus cereus mutant defective in spore coat deposition. 676 5

The inducible cholinesterase of Pseudomonas aeruginosa strain K (ATCC 25102) degraded propionylcholine, acetylthiocholine, acetylcholine and acetyl-beta-methylcholine at a high rate and butyrylcholine and succinylcholine at very low rates. The localization of the enzyme in the periplasmic space was indicated by a similar rate of acetylcholine degradation by intact cells or their extracts, by release of cholinesterase together with alkaline phosphatase into the culture medium during cell growth in a low phosphate-containing medium, by liberation of cholinesterase and alkaline phosphatase during lysozyme-induced conversion of cells to spheroplasts and by freezing and thawing. Threatment of cells with diazo-7-amino-1,3-naphthalenedisulphonic acid, which inactivates surface-located enzymes, abolished most of the cholinesterase and 5'-nucleotidase activities.
J Gen Microbiol 1980 Mar
PMID:Localization of cholinesterase in Pseudomonas aeruginosa strain K. 677 68

Rates of lysis by lysozyme (expressed as the decrease in A550 min-1) of synchronously dividing cells of Bacillus subtilis rose in concert with the stepwise increase in cell numbers. Asynchronously growing cells showed no periodicities in sensitivity; rates of lysis reflected the exponential increase in culture density.
J Gen Microbiol 1980 Jul
PMID:Sensitivity of synchronous cultures of Bacillus subtilis to lysozyme. 677 53

The N-acetylglutamate deacetylase (EC 3.5.1.-) from Pseudomonas aeruginosa, strain PAO1, was purified 15,000-fold to electrophoretic homogeneity. The enzyme was distinct from acetylornithinase and formylglutamate hydrolase. Its molecular weight was estimated to be 90,000 by gel filtration and by sedimentation in sucrose gradients. Electrophoresis in sodium-dodecyl sulphate gels gave a single band corresponding to a molecular weight of 44,000. N-Acetylglutamate deacetylase was L-specific and showed no peptidase activity. Among 17 N-acetyl-L-amino acids tested as substrates, N-acetyl-L-glutamine, N-acetyl-L-methionine and N-acetylglycine were hydrolysed at 20% of the rate of N-acetyl-L-glutamate whereas other N-acetyl-L-amino acids were deacetylated at a rate of less than 10%. The catalytic activity depended on Co2+. The Km of the enzyme with respect to N-acetylglutamate was 1.43 mM. Preparation of spheroplasts with lysozyme in the presence of 0.2 M-MgCl2 led to the release of 80% of the enzyme activity from the cells, indicating the periplasmic localization of N-acetylglutamate deacetylase. Its localization in the periplasmic space explains the inability of P. aeruginosa argA mutants to grow on N-acetylglutamate, which is utilized by the wild-type as a carbon and nitrogen source.
J Gen Microbiol 1981 Jul
PMID:Properties and localization of N-acetylglutamate deacetylase from Pseudomonas aeruginosa. 680 Nov 90

Outer membrane fractions of Moraxella nonliquefaciens 7784 strains SC-c and N-b, isolated by extraction with lithium acetate, were analysed by SDS-PAGE. Three main proteins were found, of which one, with an apparent molecular weight of 19500, was undetectable in membranes isolated by lysis of lysozyme/EDTA spheroplasts. All three major proteins were heat modifiable.
J Gen Microbiol 1983 Mar
PMID:Studies on outer membrane proteins of Moraxella nonliquefaciens. 687 14

Bacteriophage P2 is known for its exceptionally low rate of spontaneous (non-integrative) recombination, which however may be stimulated by ultraviolet irradiation of the phage. We show here that ligated dimers, made in vitro from mixtures of DNAs of two P2 mutants, upon transfection of lysozyme-spheroplasts give origin to recombinants at high frequency. While spontaneous P2 recombination occurs independently of the main recombination pathway of the bacteria, P2 recombinant formation following either ultraviolet irradiation or transfection with DNA dimers requires at least some element of such a pathway, since it is absent or greatly reduced in recA- bacteria or spheroplasts. It would seen that, in the course of its lytic development, P2 deploys a mechanism that inhibits the main recombination pathway of the host cell, or assumes DNA configurations refractory to it.
Mol Gen Genet 1980 Apr
PMID:Recombination in bacteriophage P2: recA dependent enhancement by ultraviolet irradiation and by transfection with mixed DNA dimers. 692 45

Escherichia coli ML308 225 was killed and lysed by human serum. Bacterial sensitivity to serum was maximal for organisms in the early-exponential phase of batch culture and declined as growth proceeded. Bacterial killing was dependent upon the complete complement sequence and the subsequent action of serum lysozyme caused bacteriolysis. Purified lipopolysaccharide from this organism bound to serum-sensitive bacteria and inhibited the bactericidal reaction.
J Gen Microbiol 1980 Mar
PMID:The effect of purified lipopolysaccharide on the bactericidal reaction of human serum complement. 699 28

Wall-deficient forms of Mycobacterium aurum were prepared by agitating the cells during exponential growth with D-cycloserine, glycine, lysozyme, EDTA and LiCl for approximately the time of three cell divisions (18 h). Wall-deficient forms were then converted to spheroplasts by gentle stirring with lysozyme and EDTA in a Tris/HCl buffer containing sucrose until all the cells appeared spherical by phase contrast microscopy. Subsequent lysis by nucleases followed by osmotic shock produced membrane vesicles. Ultrastructural and chemical properties of the spheroplasts and membrane vesicles are described. The spheroplasts were susceptible to lysis by 0.25% (w/v) sodium dodecyl sulphate and were permeable to certain enzyme substrates.
J Gen Microbiol 1981 May
PMID:Ultrastructural and chemical studies on wall-deficient forms, spheroplasts and membrane vesicles from Mycobacterium aurum. 703 68

Lysozyme has been studied in insects as part of the system of inducible antibacterial defence in the haemolymph. We recently found two Drosophila lysozyme genes that are constitutively expressed in the digestive tract, and are probably involved in the digestion of bacteria in the food. To obtain an overview of the lysozyme genes in this species and their possible roles in immunity and digestion, we have now characterized all six lysozyme genes in the cloned part of the lysozyme locus at 61F, and a seventh gene that maps to the same chromosomal location. The expression of the genes follows four different patterns: firstly, four closely related genes, LysB, C, D and E, are all strongly expressed in the midgut of larvae and adults; secondly, LysP is expressed in the adult salivary gland; thirdly, LysS is expressed mainly in the gastric caecae of larvae; and finally, LysX is primarily expressed in the metamorphosing midgut of late larvae and early pupae. The LysD-like genes and LysS are strongly repressed in artificially infected animals, possibly reflecting a malaise reaction in the digestive tract. None of the genes is expressed in the fat body or haemocytes. Thus rather than being a component of the haemolymph, the Drosophila lysozymes are found mainly in the digestive tract where they are expressed at a high level. Furthermore all genes, except LysP, encode acidic proteins, in contrast to the strongly basic "typical" lysozymes. This is highly reminiscent of the situation in ruminants, where the lysozymes have been recruited for the digestion of symbiotic bacteria in the stomach.
Mol Gen Genet 1994 Jan
PMID:The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract. 815 65


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