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)

Optimal conditions for detecting staphylokinase, phosphatase, protease, lipase, esterase, egg yolk factor, lysozyme, deoxyribonuclease, hyaluronidase, penicillinase, and alpha-, beta-, and delta-hemolysins in cell-free filtrates of selected strains of staphylococci by agar plate methods were established by studying the effect of factors such as buffer composition, pH, ionic strength, type of agar, nature and concentration of substrate, and certain metal ions. The final tests that evolved from this study are simple to perform, require only 6 mul of the sample per test, and are capable of detecting microgram and, in some cases, nanogram quantities of the product. The zones of reaction can also be quantitatively related to the amount of material present. The test may also be useful for the detection of extracellular products of other microorganisms.
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PMID:Agar plate tests of enhanced sensitivity for detecting biologically active products of staphylococcal filtrates. 18 61

The extracellular production of hyaluronidase and chondroitin sulfatase was demonstrated in all of the subspecies of Bacteroides fragilis tested with the exception of B. fragilis subsp. vulgatus. Elastase was found only in one strain of B. coagulans tested. This appears to be the first report of these enzyme activities in this genus. Additional enzymes found to be produced by certain members othis genus were fibrinolysin, penicillinase, lysozyme, lecithinase, deoxyribonuclease, phosphatase, protease, and lipase.
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PMID:Extracellular enzymes of the genus Bacteroides. 18 84

Three methods at present available for the purification of staphylococcal delta-haemolysin were compared as to the purity and identify of the product obtained. None yielded a pure preparation of delta-haemolysin; one of the three preparations did not contain demonstrable delta-haemolysin when tested electrophoretically, but it contained deoxyribonuclease, penicillinase, phosphatase and alpha-haemolysin. The second preparation had delta-haemolysin activity and was free of alpha-haemolysin, but it contained lipase, egg-yolk factor, esterase, deoxyribonuclease, penicillinase, phosphatase and hyaluronidase. The third preparation contained all of the products mentioned above, except phosphatase, and it also contained alpha-haemolysin, staphylokinase, lysozyme and caseinase. These findings are discussed with special reference to the requirement for criteria of purity in work with staphylococcal products.
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PMID:Purity of staphylococcal delta-haemolysin obtained by three different procedures. 18 51

Data on the role of oral lysozyme, ribonuclease, deoxyribonuclease and peroxidase in antimicrobial defense of the macroorganism are reviewed. The biochemical and physiological properties of the enzymes secreted by salivary glands and released from emigrating leukocytes are discussed. Spectra of antimicrobial action of the enzymes and participation of these enzymes in maintaining the stability of oral biocenosis are described as well as the regulation of these enzymatic activities and the pathogenetic significance of impairments in their secretion. The most perspective aspects of the problems discussed are outlined for further investigation.
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PMID:[Enzymatic mechanisms for antimicrobial protection of the oral cavity]. 20 88

Vibrio cholerae phage PL 163/10, belonging to Mukherjee's group I, gave clear plaques with surrounding halos of overall diameters varying between 1 to 4 mm when plated on a lawn of host V. cholerae OGAWA 154. It was fairly stable in the PH range 6-11. Its thermal inactivation was characterised by half lives of 39, 12, 4.5 and 1.0 minutes at 55, 60, 65 and 70 degree C respectively. The thermodynamic parameters deltaH, deltaF and deltaS were determined at these temperatures. The phange was resistant in vitro to sodium deoxycholate, trytrypsin, chloroform, robonuclease, deoxyribonuclease, Tris, Tris + EDTA, Tris + lysozyme and phosphate buffer but rapidly inactivated by sodium lauryl sulfate. Adsorption of this phage was biphasic. Intracelllular growth of the PL 163/10 phage was characterised by an eclipse period of 13 minutes, latent period of 31 minutes, rise period of 29 minutes and an average burst size of about 10 PFU/cell. This phage possessed a hexagonal head 106 plus or minus 18 x x 740 plus or minus 27 A without any tail structure.
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PMID:Properties of the cholera phage PL 163/10. 23 74

About 60 characteristics have been investigated in 7 hemolyzing and 12 nonhemolyzing strains of L. monocytogenes. From these investigations resulted inter alia that the organism grows well under strictly anaerobic conditions, esculin is split at 45 degrees C,NH3 is produced from peptone, but not from arginin, and H2S can be traced by sufficiently sensitive methods. All strains possess a lipase, muramidase, and deoxyribonuclease, the hemolytic ones only also a lecithinase. Besides, the hemolytic strains only dispose of experimental virulence and of a CAMP factor-like agent. The experimental animal of choice seems to be the conjunctivally infected guinea pig in which a generalized infection develops.
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PMID:[Some properties of carrier strains of Listeria monocytogenes (author's transl)]. 81 65

The biotyping scheme of Baird-Parker was applied to cultures of Staphylococcus epidermidis from patients. In all, 63.6% of 228 cultures belonged to biotype 1, followed by biotypes 4, 3, and 2 in decreasing order of incidence. When classified according to clinical source of isolation, cultures of S. epidermidis were most frequently isolated from urine, with 39.5% of 228 cultures from this source. Each of the four biotypes was distributed throughout all nine catagories of clinical sources. The production of virulence factors was based on the results of three groups of tests: (i) deoxyribonuclease, urease, gelatinase, caseinase, and lysozyme production; (ii) lipolytic activity on the tweens; and (iii) hemolysin production. Enzymatic activity was highest for organisms in biotypes 1, followed by biotypes 3, 4, and 2 in decreasing order. Of the 228 cultures, 76.3% were lysed by lysostaphin. Resistance to antibiotics was highest for tetracycline, ampicillin, and penicillin, with rates of 54.8, 69.3, and 81.6%, respectively. The role of S. epidermidis as an etiological agent was studied by analyzing the laboratory and clinical data of 80 patients selected at random with bacteriuric S. epidermidis. Organisms in biotype 1 were most commonly associated with urinary tract infection. The significance of certain biotypes of S. epidermidis as opportunistic pathogens among compromised hosts in a hospital environment is discussed.
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PMID:Virulence factors of biotypes of Staphylococcus epidermidis from clinical sources. 117 3

Mediators released from injured human skin that initiate the inflammatory response have not been adequately identified. Organ culture of full-thickness skin explants enables us to do so, because injury to the skin can be made in vitro, eliminating the rapid leakage of serum and infiltration of leukocytes that occur in vivo. In our studies, the military vesicant sulfur mustard (SM) (10 microliters of a 0.01 to 1.0% dilution) was topically applied to injure the epidermis of the explant. Then, the explants were cultured in small Petri dishes, usually for 18 h at 36 degrees C, and the organ-culture fluids were assayed for various inflammatory mediators. We found that the culture fluids from SM-exposed and control explants contained similar amounts of angiotensin-converting enzyme, trypsin-like and chymotrypsin-like proteases, acid phosphatase, beta-glucuronidase, beta-galactosidase, lysozyme, deoxyribonuclease, ribonuclease, interleukin 1, and lactic dehydrogenase. However, the culture fluids from SM-exposed explants contained increased amounts of histamine and plasminogen-activating activity, and often prostaglandin E2, when compared to culture fluids from control explants. After 3 to 4 d in culture, full-thickness human skin explants, when exposed to 0.2% SM (but not when exposed to 1.0% SM), sometimes showed separation of the epidermis and increased collagenase activity (i.e., hydroxyproline release). Thus, histamine (from local mast cells), and prostaglandin E2 and plasminogen-activating activity (probably from both mast cells and epidermal cells) are apparently involved in early mediation of the inflammatory response.
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PMID:Mediators, initiating the inflammatory response, released in organ culture by full-thickness human skin explants exposed to the irritant, sulfur mustard. 171 Jun 39

Replacement of the amino-terminal 40-amino-acid region of the 588-amino-acid precursor of the membrane-bound penicillin-binding protein 3 (PBP3) by the decapeptide MKGKEFQAWI was carried out by altering the amino-coding end of the ftsI gene. Insertion of the modified gene into a runaway-replication plasmid under the control of a fused lpp promoter and lac promoter/operator, resulted in the overexpression by Escherichia coli of the modified PBP3 (designated PBP3**) in the cytoplasm. About 80% of the accumulated PBP3** underwent sequestration in the form of insoluble protein granules that were isolated by cell breakage or cell lysis. After selective removal of contaminants by an EDTA-lysozyme/DNase (deoxyribonuclease)/Nonidet extraction, treatment of the granules with guanidinium chloride followed by dialysis against buffer containing 0.5 M NaCl yielded a refolded, water-soluble PBP3**, which, upon chromatography on Superose 12, exhibited the expected 60,000 molecular mass. The refolded PBP3** bound benzylpenicillin in a 1 to 1 molar ratio, was highly sensitive to aztreonam and showed the same degree of thermostability, in terms of penicillin-binding capacity, as the parent, membrane-bound PBP3, suggesting that protein refolding occurred with formation of the correct intramolecular interactions. Two to three mg of refolded PBP3** can be obtained from 1 litre of culture of the overproducing strain.
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PMID:Overexpression, solubilization and refolding of a genetically engineered derivative of the penicillin-binding protein 3 of Escherichia coli K12. 305 Mar 60

Mycobacterium paratuberculosis, the causative agent of paratuberculosis, produces considerable economic loss in the cattle industry in many countries. The slow growth of M. paratuberculosis has hindered investigations of the antigenic composition of the organism and the development of species-specific antigen for serological detection of this disease. This paper describes a simple method for the isolation of large quantities of viable M. paratuberculosis from the intestinal mucosa of infected cattle by a combination of trypsin digestion, deoxyribonuclease/lysozyme treatment and differential centrifugation. Purity was about 99% and yield between 10(5)-10(9) bacteria/g tissue.
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PMID:A technique for the purification of Mycobacterium paratuberculosis from the ileal mucosa of infected cattle. 353 28


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