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  • Articles  (34)
  • Blackwell Publishing Ltd  (19)
  • Hindawi  (12)
  • Blackwell Science Ltd
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  • Articles  (34)
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  • 1
    Electronic Resource
    Electronic Resource
    Reproduction of interspecific hybrids of Atlantic salmon and brown trout in a stream environment (2003)
    Oxford, UK : Blackwell Science Ltd
    Freshwater biology 48 (2003), S. 0 
    Details
    ISSN: 1365-2427
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: 1. Reproduction between Atlantic salmon males and interspecific hybrid Salmo salar × Salmo trutta females was monitored in a controlled flow channel diverted from a south European river located at the edge of Atlantic salmon natural geographic distribution in Europe.2. Post-F1 hybrids were viable and survived in the wild, at least until dispersal from redds. After transfer to hatchery conditions, 67% survived into the second year.3. The hybrids possessed 98 chromosomes: two sets of Atlantic salmon(2n = 58) and one set of brown trout (n = 40) chromosomes.4. The existence of a low proportion of allotriploid individuals can be expected in rivers where Atlantic salmon and brown trout populations coexist.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2427.2003.01068.x
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  • 2
    Electronic Resource
    Electronic Resource
    hns mutant unveils the presence of a latent haemolytic activity in Escherichia coli K-12 (1996)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 19 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.443955.x
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  • 3
    Electronic Resource
    Electronic Resource
    The pair of arginine codons AGA AGG close to the initiation codon of the lambda int gene inhibits cell growth and protein synthesis by accumulating peptidyl-tRNAArg4 (2003)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 49 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: To analyse the mechanism by which rare codons near the initiation codon inhibit cell growth and protein synthesis, we used the bacteriophage lambda int gene or early codon substitution derivatives. The lambda int gene has a high frequency of rare ATA, AGA and AGG codons; two of them (AGA AGG) located at positions 3 and 4 of the int open reading frame (ORF). Escherichia coli pth (rap) cells, which are defective in peptidyl-tRNA hydrolase (Pth) activity, are more susceptible to the inhibitory effects of int expression as compared with wild-type cells. Cell growth and Int protein synthesis were enhanced by overexpression of Pth and tRNAArg4 cognate to AGG and AGA but not of tRNAIle2a specific for ATA. The increase of Int protein synthesis also takes place when the rare arginine codons AGA and AGG at positions 3 and 4 are changed to common arginine CGT or lysine AAA codons but not to rare isoleucine ATA codons. In addition, overexpression of int in Pth defective cells provokes accumulation of peptidyl-tRNAArg4 in the soluble fraction. Therefore, cell growth and Int synthesis inhibition may be due to ribosome stalling and premature release of peptidyl-tRNAArg4 from the ribosome at the rare arginine codons of the first tandem, which leads to cell starvation for the specific tRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03611.x
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of Sodium Chloride, Acetic Acid, and Enzymes on Carotene Extraction in Carrots (Daucus carota L.) (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Carrot root cores were cut off longitudinally and treated with NaCl (0.6 and 1.2 M) and/or acetic acid (1.33%, 2.67%, and 4%) solutions. The extractability of the carotenes was estimated. Similarly, carrot cores were also treated with some degrading enzymes (carbohydrases, lipases, and proteases) alone or in combination to study the effect of the tissue rupture or the hydrolysis of possible complexes or interactions between carotenes and other components on the carotene extractability. The results showed that acetic acid increased the extractability of α- and β carotenes up to 99.8% and 94.6%, respectively, at a 4% acid concentration compared with the samples without any treatment. This increase was directly proportional to the acid concentration. An increase in extractability was also observed for NaCl, although the increases were not as high as in the previous case with values of 49% and 41.4% for α- and β-carotenes respectively at a 0.6 M concentration. The study of microstructural changes and extractability revealed that the enzymatic treatments could have broken some carotene complexes and interactions and altered the carbohydrate matrix structure, increasing to a certain extent the extractability of carotenes. It can be concluded then that pickling with 4% acetic acid is a good method to increase the extractability of α- and β-carotenes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb07118.x
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  • 5
    Electronic Resource
    Electronic Resource
    Proteolysis of ribulose-1,5-bisphosphate carboxylase/oxygenase in Citrus leaf extracts (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 66 (1986), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBP carboxylase, EC 4.1.1.39) has been purified from orange [Citrus sinensis (L.) Osbeck cv. Washington Navel] leaves using sucrose gradient centrifugation in a fixed angle rotor. Following sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), two major bands corresponding to the two subunits of RuBP carboxylase were found. The large subunit coincided with the polypeptide band that has been previously reported to be preferentially mobilized during the spring and summer flush periods.The degradation of RuBP carboxylase during autodigestion of Citrus leaf extracts, investigated by SDS-PAGE, occurred mainly at acidic (2.5-5.5) pH. The two subunits showed differences in the rate of degradation, the smaller being more rapidly hydrolyzed than the larger. At least four proteolytic activities were identified by means of inhibitor experiments: 1) a pepstatin A-sensitive activity that acts on both RuBP carboxylase subunits, 2) a mercurial (p-hydroxymercuribenzoate and p-chloromercuriphenylsulfonate)-sensitive activity that degrades only the small subunit, 3) an EDTA-sensitive activity that hydrolyzes both the large and small subunits, and 4) a mercurial-stimulated activity that acts only on the large subunit. It is suggested that the last two proteases may be responsible for the degradation of RuBP carboxylase observed in vivo during the periods of mobilization of leaf protein in Citrus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1986.tb05938.x
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  • 6
    Electronic Resource
    Electronic Resource
    Extraction of tracheal sap from Citrus and analysis of its nitrogenous compounds (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 50 (1980), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Tracheal sap was extracted from sections of stems (0.5 to 1.5 cm in diameter and 7.5 to 15.0 cm in length) of orange trees (Citrus sinensis (L.) Osbeck cv. Washington Navel) by using a combination of the vacuum and liquid displacement methods. The volume of sap obtained and its concentration of nitrogenous compounds were dependent on the volume of displacing liquid used for the extraction. Four ml of water-saturated 1-butanol extracted essentially all of the xylem fluid present in the stem sections without apparent production of artifacts.The time of sampling affected the nitrogen concentration of the tracheal sap, but not the content of xylem nitrogen per volume of stem material. The orientation of the stems in the tree and the diameter of the stems had an effect on their contents of xylem nitrogen, with southeastern orientation and thinner stems showing higher concentrations.We could not detect the presence of ammonium, nitrites or proteins in the tracheal sap of orange trees. Most of the nitrogen was present as amino acids and about 2% of the total in the form of nitrates. The qualitative composition of amino acids, as determined by TLC, was the same both in winter and spring tracheal sap. The main components of the sap were proline and arginine in winter, and these amino acids together with asparagine and aspartic acid in spring.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1980.tb04466.x
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  • 7
    Electronic Resource
    Electronic Resource
    Clinical strains of Candida albicans express the surface antigen glyceraldehyde 3-phosphate dehydrogenase in vitro and in infected tissues (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 23 (1999), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have previously described the presence of an enzymatically active form of glyceraldehyde 3-phosphate-dehydrogenase (GAPDH) in the cell surface of Candida albicans ATCC 26555 which is also a fibronectin and laminin binding protein. Immunohistochemical analysis of tissue sections from patients with disseminated candidiasis with a polyclonal antiserum to GAPDH from C. albicans (PAb anti-CA-GAPDH) revealed that the enzyme is expressed at the surface of fungal cells in infected tissues. The same PAb detected the presence of GAPDH species, with a molecular mass of approximately 33 kDa, in cell wall extracts obtained from clinical isolates of the fungus. These cell surface-bound GAPDH moieties exhibited a dose-dependent dehydrogenase activity. These results indicate that this cell surface-bound GAPDH plays a role during infection, probably contributing to the attachment of fungal cells to host tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1999.tb01243.x
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  • 8
    Electronic Resource
    Electronic Resource
    The C-terminal antibody binding domain of Candida albicans mp58 represents a protective epitope during candidiasis (2004)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 232 (2004), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The 58-kDa surface mannoprotein of Candida albicans (mp58) elicits strong antibody responses during infection. Epitope mapping with sera from patients with candidiasis and control individuals indicated the presence of multiple IgG-reactive continuous epitopes on the protein, expanding both the amino- and carboxy-terminal domains and several internal regions. These immunoreactive regions were similar to the ones previously identified using sera from immunized animals. Two of the epitopic regions (including the C-terminal domain) showed increased reactivity with antibodies present in sera from patients with candidiasis as compared to control individuals. Patients who survived the infection displayed increased antibody reactivity towards the C-terminal epitope as compared to those succumbing to candidiasis. A monoclonal antibody directed towards this epitopic region conferred protection in serum therapy experiments in a murine model of hematogenously disseminated candidiasis. Together, these observations indicate the carboxy-terminal antibody binding domain of C. albicans mp58 represents a protective epitope during candidiasis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(04)00042-4
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  • 9
    Electronic Resource
    Electronic Resource
    Transcriptional regulation of mexR, the repressor of Pseudomonas aeruginosa mexAB-oprM multidrug efflux pump (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 207 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The transcription start site of mexR, encoding the repressor of the Pseudomonas aeruginosa mexAB-oprM multidrug efflux pump, has been determined by S1 mapping. One signal corresponding to a single promoter has been found, whereas three major signals were observed for the mexA messenger. Further analysis demonstrated that mexA has just one promoter that overlaps with the mexR promoter, with the other two signals observed by S1 probably being the consequence of RNA processing. Transcription of mexR and mexA from the aforementioned promoters is regulated by MexR. We show that bacterial growth phase affects expression of these promoters as well. mexR expression was higher at the exponential growth phase and declined afterwards, whereas mexA expression was triggered at the onset of the stationary growth phase. A model for the regulation of mexR and mexA expression, which includes an analysis of the interplay between both promoters, is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11029.x
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  • 10
    Electronic Resource
    Electronic Resource
    Growth of Escherichia coli in acetate as a sole carbon source is inhibited by ankyrin-like repeats present in the 2′,5′-linked oligoadenylate-dependent human RNase L enzyme (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 149 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Expression of low levels of the 2′,5′-linked oligoadenylate-dependent human RNase L, an enzyme induced by interferons, is highly toxic in Escherichia coli. This protein contains an ankyrin domain responsible for RNase L toxicity. The only known ORF in E. coli containing ankyrin repeats is yjaC in the acetate metabolic cluster. We have investigated if expression of mutant forms of RNase L interfere with metabolism of acetate in E. coli. Our findings demonstrate that E. coli expressing RNase L ankyrin repeats is unable to grow in medium containing acetate as the sole carbon source, while it can grow when expressing other domains of the protein. This defect correlates with a severe decrease in the levels of induction of enzymes in the glyoxylate bypass.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10316.x
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