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  • Springer  (21)
  • Oxford University Press  (10)
  • Blackwell Publishing Ltd  (7)
  • 1985-1989  (38)
  • 1988  (38)
  • 1
    Electronic Resource
    Electronic Resource
    Narcolepsy and HLA in the Japanese (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 540 (1988), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1988.tb27056.x
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation and characterization of enterotoxigenic Escherichia coli mutants that produce abnormal heat-labile enterotoxins (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 51 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Mutants (LT mutants) of enterotoxigenic Escherichia coli that produced heat-labile enterotoxin (LT), differing immunologically and functionally from native LT, were obtained by N-methyl-N′-nitro-N-nitrosoguanidine treatment. On screening 1000 colonies by the Biken test, 10 mutants were obtained.Two of these mutants did not produce LT; two produced biologically active LT that differed immunologically from native LT, one mutant produced the A subunit, but not the B subunit; three produced LTs that were composed of A and B subunits but were biologically inactive and differed immunologically from native LT.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02970.x
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  • 3
    Electronic Resource
    Electronic Resource
    Hemagglutinating activity of the B subunit(s) of the heat-labile enterotoxin isolated from human enterotoxigenic Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The hemagglutinating activity of the B subunit(s) of the heat-labile toxin (LTh - B) produced by human enterotoxigenic Escherichia coli was studied by hemagglutination and hemagglutination inhibition. Very strong hemagglutination of both neuraminidase- and pronase-treated human erythrocytes was induced by the LTh - B whereas that of intact ones was induced weakly or not at all by the LTh - B at the highest concentration used. Enhancement in hemagglitination of these human erythrocytes by the LTh - B was about 8- to 512-fold for type A and B erythrocytes and 16-fold for type O erthrocytes, respectively. On the other hand, no hemagglutination of intact and treated sheep erythrocytes was found by the LTh - B at the highest concentration used. Hemagglutination of pronase-treated human type B erythrocytes by the LTh - B was inhibited by galactose and melibiose among mono-, di- and polysaccharides used as inhibitors. These findings suggest that the LTh - B is a bacterial lectin specific for galactose-linked residues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02777.x
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and characterization of heat-labile enterotoxin isolated from chicken enterotoxigenic Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 52 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The heat-labile enterotoxin (LTc) isolated from chicken enterotoxigenic Escherichia coli was purified to homogeneity and its molecular and antigenic properties were compared with those of purified LTs from porcine and human enterotoxigenic Escherichia coli (LTp, LTh). The A subunit of LTc was identical to that of LTp and the B subunit of LTc was identical to that of LTh but not that of LTp, in mobility on SDS-polyacrylamide gel electrophoresis. Ouchterlony tests demonstrated that LTc is antigenically identical to LTh but not with LTp. The pI point and amino acid composition of LTc were also compared and the results suggest that chicken enterotoxigenic E. coli produced an LT similar to LTh.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02575.x
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  • 5
    Electronic Resource
    Electronic Resource
    Hemagglutinating activity of the heat-labile enterotoxin isolated from porcine enterotoxigenic Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The hemagglutinating activity of the heat-labile enterotoxin (LTp) isolated from porcine enterotoxigenic Escherichia coli was studied by hemagglutination inhibition. The hemagglutinating activity of LTp was enhanced 64–512-fold with pronase- and neuraminidase-treated human erythrocytes although both intact human and sheep erythrocytes were not agglutinated by LTp at the highest concentration used. No enhancement was found in hemagglutination of neuraminidase-treated sheep erythrocytes by LTp. Hemagglutination of pronase-treated human type A erythrocytes induced by LTp was inhibited by melibiose and galactose among mono-, di-, and polysaccharides used as inhibitors. Galactose was a slightly better inhibitor than melibiose. These findings suggest that LTp is a bacterial lectin specific for galactose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02712.x
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of nicking on Shiga-like toxin I of enterohaemorrhagic Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 56 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The Shiga-like toxin I (SLT-I), which had an unnicked A subunit, was purified from Escherichia coli O157: H7. After incubation of the unnicked SLT-I with trypsin, the A subunit of the toxin was nicked and converted to A1 and A2 peptides, which were linked by the disulfide bond. The effects of nicking of SLT-I on its heat stability and cytotoxic activity against Vero cells were examined. The trypsin treatment of SLT-I neither reduced nor increased the ability of cytotoxic activity or the heat stability of the toxin. The time course of binding of the toxin to Vero cells also was not affected by nicking of the toxin. These results indicate the absence of a difference in biological or physical properties of SLTs between nicked and unnicked conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb03158.x
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  • 7
    Electronic Resource
    Electronic Resource
    Evidence of common epitopes in the ganglioside binding site of Vibrio cholerae and Escherichia coli heat-labile enterotoxins (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Twenty monoclonal antibodies (mAbs) reacting with cholera toxin (CT) of Vibrio cholerae strain 569B were characterized in cross-section and GM1 ganglioside inhibition assays. MAbs were characterized by reaction with CT and Escherichia coli heat-labile porcine strain (LTp) and human strain (LTh) enterotoxins, and by GM1 ganglioside inhibition of mAb binding. Eight of 10 CT-A specific and 3 of 10 CT-B-specific mAbs cross-reacted with LTh and LTp. GM1 ganglioside inhibited reactions of the CT-B cross-reacting antibodies. Results showed that these epitodes common to the B subunit of CT and LT are located in or near the GM1 ganglioside binding region, and that the GM1 ganglioside-binding region of LT differs from that of CT.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02673.x
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  • 8
    Electronic Resource
    Electronic Resource
    Unusual sequences, homologous to 5S RNA, in ribosomal DNA repeats of the nematodeMeloidogyne arenaria (1988)
    Springer
    Journal of molecular evolution 27 (1988), S. 222-227 
    Details
    ISSN: 1432-1432
    Keywords: Ribosomal DNA ; 5S RNA ; Nematode ; Molecular phylogeny ; Progenote ; Gene families
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary There are sequences homologous to 5S ribosomal RNA in the ribosomal DNA (rDNA) repeats of the plant-parasitic nematodeMeloidogyne arenaria. This is surprising, because in all other higher eukaryotes studied to date, the genes for 5S RNA are unlinked to and distinct from a tandem rDNA repeat containing the genes for 18S, 5.8S, and 28S ribosomal RNA. Previously, only prokaryotes and certain “lower eukaryotes” (protozoa and fungi) had been found to have both the larger rRNAs and 5S rRNA represented within a single DNA repeat. This has raised questions on the organization of these repeats in the earliest cell (progenote), and on subsequent evolutionary relationships between pro- and eukaryotes. Evidence is presented for rearrangements and deletions withinMeloidogyne rDNA. The unusual life cycles (different levels of ploidy, reproduction by meiotic and mitotic parthenogenesis) of members of this genus might allow rapid fixation of any variants with introduced 5S RNA sequences. The 5S RNA sequences inMeloidogyne rDNA may not be expressed, but their presence raises important questions as to the evolutionary origins and stability of repeat gene families.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02100078
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  • 9
    Electronic Resource
    Electronic Resource
    Histone genes in three sea star species: Cluster arrangement, transcriptional polarity, and analyses of the flanking regions of H3 and H4 genes (1988)
    Springer
    Journal of molecular evolution 27 (1988), S. 36-44 
    Details
    ISSN: 1432-1432
    Keywords: Histone genes ; Sea stars ; Echinoderms ; Evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The arrangement of core histone genes and their transcriptional polarity has been determined for three species of sea stars (Pisaster ochraceus, P. brevispinus, andDermasterias imbricata) representing two orders which diverged over 500 million years ago. Each species has approximately 500 core histone cluster repeats per haploid genome. The close phylogenetic relationship between thePisaster species is evident from the correspondence of restriction sites in the repeat element, identical arrangement of core histones, and high degree of sequence homology in both the coding and spacer regions of the H3 gene. TheDermasterias repeat has the same gene order and transcriptional polarity of core histones, but its restriction map is significantly different. Moreover, theDermasterias H3 gene has the same amino acid sequence, but in comparison toPisaster nucleotide sequences, shows a high level of silent substitutions. Analyses of the nucleotide sequence of the 5′ and 3′ regions surrounding the H3 gene from each species demonstrate the presence of appropriately spaced consensus and processing signal segments. The 3′ spacer segment of theDermasterias H4 gene contains an unusual, threefold tandemly repeated, 21-nucleotide, AT-rich sequence. No similar sequence is seen in theP. brevispinus H4 3′ region, but these two species show a striking regularity of distribution of five different homologous oligomers in the 3′ spacer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02099728
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  • 10
    Electronic Resource
    Electronic Resource
    Isolation of a new cellulase gene from a thermophilic anaerobe and its expression inEscherichia coli (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 264-268 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A new cellulase gene was cloned and expressed inEscherichia coli from a thermophilic anaerobe, strain NA10. A 7.4 kbEcoRI fragment of NA10 DNA encoded the cellulase which hydrolyzed carboxymethyl cellulose, lichenan, andp-nitrophenyl-β-d-cellobioside, but could not digest laminarin andp-nitrophenyl-β-d-glucoside. The cloned enzyme could digest cellooligosaccharides and release cellobiose as a main product from cellotetraose but could not digest cellobiose. It was distinct from the endoglucanase which was cloned by us previously from NA10 strain in terms ofp-nitrophenyl-β-d-cellobioside degradation activity and the location of restriction enzyme sites. The enzyme produced byE. coli transformant was extremely heat-stable and the optimum temperature for the enzymatic reaction was 80°C. Fifty three percent of the cloned enzyme was detected in the periplasm and the remaining activity existed in the cellular fraction in theE. coli transformant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00939319
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