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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 108 (1976), S. 271-279 
    ISSN: 1432-072X
    Keywords: Bacteriophage ; Myxococcus ; DNA ; Restriction ; Phage proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Phage-like particles were found in the supernatants of cultures of strains of Myxococcus xanthus, M. virescens and M. fulvus. The largest number of such particles was associated with M. virescens V2. Most of the particles were similar in morphology to the virulent Myxococcus phage, MX-1. 2. Several new phages were isolated from soil and animal droppings. A new phage was isolated from cultures of M. virescens V2. All resembled phage MX-1 in morphology and were related to phage MX-1 serologically. One of these phage, øm, was characterized by fractionation of its proteins by SDS-polyacrylamide gel electrophoresis and by analysis of the restriction fragments of its DNA. The very close relatedness with MX-1 was confirmed by these techniques. Phage øm, was found to exist in a state of pseudolysogeny with strains of M. virescens and M. fulvus. 3. Two types of bacteriocin-like activity were found associated with Myxococcus strains. In one case, the activity was extracted from chloroform-killed or from sonicated cells. In the second case it was associated with extracellular material. Strains of Salmonella and Cytophaga were found to be good indicators for this latter activity. These strains were found to be killed by phage MX-1. 4. The significance of these data for origin of the phages of myxococci are discussed and it is proposed that MX-1 and the newly isolated phages may be virulent mutants of a family of lysogenic phages.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 108 (1976), S. 221-226 
    ISSN: 1432-072X
    Keywords: Bacteriophage MX-1 ; Myxococcus ; DNA ; Restriction fragments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Bacteriophage MX-1 is a virulent DNA phage whose hosts include strains of Myxococcus xanthus, M. fulvus and M. virescens. DNA was extracted from purified phage preparations. The molecular weight of phage DNA was measured by sedimentation-velocity and by rate-zonal ultracentrifugation. The apparent molecular weight was found to vary for reasons discussed in the text. From ratezonal ultracentrifugation, using calibrated sucrose gradients, the molecular weight was calculated to be 149 (± 22)×106 daltons. The base composition of the DNA was estimated by different methods and was found to be 50–52% (G+C). The DNA demonstrated an anomalous thermal denaturation profile in dilute buffer. Denatured DNA was fractionated by ion-exchange chromatography and by buoyant-density centrifugation. No significant strand separation was obtained and it was concluded that overall base compositions of the two strands are very similar. 2. DNA from bacteriophage MX-1 was hydrolysed with restriction endonucleases R. EcoRI, R. EcoRII and R. HindIII. The restriction fragments were catalogued and their apparent molecular weights calculated from electrophoresis gels calibrated with fragments from the DNA of coliphage λ. From the total fragments obtained with nuclease R. EcoRI, the minimum apparent molecular weight of MX-1 DNA was found to be 130×106 daltons.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Environment and Resources 5 (1980), S. 389-412 
    ISSN: 0362-1626
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 10 (1971), S. 456-459 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 41 (1937), S. 1183-1193 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In order to investigate the basis of functional diversity among the pyridine nucleotide-oxidoreductases the gor gene from Pseudomonas aeruginosa PAO, which encodes glutathione reductase, was analysed. The P. aeruginosa gor gene was identified by hybridization with a short DNA sequence from the gene encoding mercuric reductase in transposon Tn501. The gene was cloned, sequenced and overexpressed in Escherichia coli. Expression of the gene enabled rescue of an E. coli gor- mutant, confirming the identity of the cloned gene. The predicted sequence of the gene product showed homology with other members of the pyridine nucleotide-disulphide oxidoreductase family, and allowed determination of positions that may be involved in substrate specificity. These predictions provided information on the relationship of sequence to function, independently of structural data used in previous studies.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A DNA sequence for the genome of bacteriophage φX174 of approximately 5,375 nucleotides has been determined using the rapid and simple ‘plus and minus’ method. The sequence identifies many of the features responsible for the production of the proteins of the nine known genes of the ...
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Sequence determination of mutants in genes A and B confirms that these constitute another pair of genes in φX174 which are translated from the same DNA sequence using different reading ...
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Two angiotensin converting enzyme (ACE) inhibitors, trandolapril and enalapril, were compared for their effects on rat food-pad oedema induced by carrageenin, bradykinin dextran and platelet activating factor (PAF). Trandolapril (0.03–30.0 mg/kg, per os) potentiated carrageenin-induced oedemas. Enalapril produced the same effect at 3–10 fold higher doses (0.3–30.0 mg/kg per os). Both ACE inhibitors were equiactive in potentiating bradykinin-induced oedema. Neither compound affected dextran-induced oedema. In marked contrast PAF-induced oedema was reduced by both ACE inhibitors, trandolapril being approximately 10 fold more active than enalapril. The observed differences in potency between the two ACE inhibitors corresponded with their previously described actions on inhibition of plasma and tissue ACE and in inducing hypotension. The results suggest a crucial role of kinins in the oedemagenic response to carrageenin. The reason why the ACE inhibitors reduced PAF-induced oedema is not clear, but could involve peripheral vasodilation.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary DNA sequences that encode the tnpR genes and internal resolution (res) sites of transposons Tn21 and Tn501, and the res site and the start of the tnpR gene of Tn1721 have been determined. There is considerable homology between all three sequences. The homology between Tn21 and Tn501 extends further than that between Tn1721 and Tn501 (or Tn21), but in the homologous regions, Tn1721 is 93% homologous with Tn501, while Tn21 is only 72–73% homologous. The tnpR genes of Tn21 and Tn501 encode proteins of 186 amino acids which show homology with the tnpR gene product of Tn3 and with other enzymes that carry out site-specific recombination. However, in all three transposons, and in contrast to Tn3, the tnpR gene is transcribed towards tnpA gene, and the res site is upstream of both. The res site of Tn3 shows no obvious homology with the res regions of these three transposons. Just upstream of the tnpR gene and within the region that displays common homology between the three elements, there is a 50 bp deletion in Tn21, compared to the other two clements. A TnpR− derivative of Tn21 was complemented by Tn21, Tn501 and Tn1721, but not by Tn3.
    Type of Medium: Electronic Resource
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