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  • 1990-1994  (5)
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  • 1
    Electronic Resource
    Electronic Resource
    Analysis of orientation distribution in YBa2Cu3O7−x polycrystals by electron channeling patterns (1990)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 68 (1990), S. 6341-6346 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A unit standard map for YBa2Cu3O7−x superconductors was constructed and indexed from a series of electron channeling patterns (ECPs). (001) pole figures of YBa2Cu3O7−x tapes and bulk specimens with various values of critical current density (Jc) were drawn by using the map covering [001-1¯1¯0-1¯10] stereographic quadrant and ECPs taken from individual grains of the specimens. It was found that preferred orientation of (001) formed in the tape with a decreasing thickness of the tape, which raised Jc significantly. It is concluded that the ECP technique is very useful for the analysis of orientation distribution in small-sized YBa2Cu3O7−x specimens such as tapes or thin films.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.346879
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular cloning of the S-layer protein gene of Campylobacter rectus ATCC 33238 (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 116 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A genomic DNA library of Campylobacter rectus (Wolinella recta) ATCC 33238 was constructed using bacteriophage lambda EMBL3 as a vector. One clone expressing the S-layer protein was identified immunologically with the antiserum to the S-layer protein of C. rectus ATCC 33238. Western immunoblotting using monoclonal antibodies directed against the S-layer protein showed a single blot of recombinant protein at 150 kDa, suggesting that this clone contained the entire coding region of the S-layer protein gene. Additionally, the S-layer protein gene was subcloned into plasmid vector pUC18. Southern hybridization revealed that the S-layer protein gene was present on the chromosome of C. rectus as a single-copy gene, and that there were minor heterogeneities among the S-layer protein genes of clinical isolates. Moreover, a spontaneous stable mutant strain, which has no S-layer expression, also conserved the full-length gene of the S-layer protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06668.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Heat shock protein 60 (GroEL) from Porphyromonas gingivalis: Molecular cloning and sequence analysis of its gene and purification of the recombinant protein (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 119 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Porphyromonas gingivalis is associated with human periodontal disease. We cloned and sequenced the gene for heat shock protein 60 (GroEL, HSP60) from P. gingivalis FDC381. The identified clone carried a 2.6 kb DNA fragment which contained two open reading frames (ORFs) encoding a 9.6- and a 58.4-kDa protein. The translated amino acid sequence of these ORFs showed a high degree of homology with known sequences for GroES and GroEL from several bacterial species and humans. Escherichia coli carrying this clone expressed a 65-kDa protein which was recognized by anti-Mycobacterium leprae HSP60 monoclonal antibody. We purified the 65-kDa protein by DEAE-sepharose chromatography and hydroxyapatite chromatography. This protein was immunogenic and was recognized by sera from a number of patients with periodontal disease. This immunological reactivity and the existence of molecular mimicry between the P. gingivalis GroEL and other HSP homologs may indicate an important role for this molecule in periodontal lesion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06879.x
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  • 4
    Electronic Resource
    Electronic Resource
    Antigenic properties of Campylobacter rectus (Wolinella recta) major S-layer proteins (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 108 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The antigenic properties of the surface layer (S-layer) proteins of various Campylobacter rectus strains including 24 clinical isolates and the type strain ATCC 33238 were examined. S-layer proteins were extracted from whole cells by acid treatment according to the method of McCoy et al. (Infect. Immun. 11, 517–525, 1975). The acid extracts from 23 of the isolates and ATCC 33238 contained two major proteins with molecular masses of 130 kDa and 150 kDa, both of which were identified as subunits of the S-layer after comparison with the protein profiles of acid-treated (S-layer-deficient) cells. An S-layer protein from one isolate (CI-808) demonstrated a different molecular mass (160 kDa). Both the 150-kDa proteins of ATCC 33238 and isolate CI-306 and the 160-kDa protein of CI-808 were purified by ion-exchange chromatography in the presence of urea. In Ouchterlony immunodiffusion experiments with these purified proteins and rabbit antiserum raised to each purified protein, both common and strain-specific antigenic determinants were identified in the C. rectus S-layer proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06115.x
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a 53 kDa major cell envelope protein antigen from Treponema denticola ATCC 35405 (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 29 (1994), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A major cell envelope protein was purified from the cell envelope fraction of Treponema denticola ATCC 35405 by ion exchange chromatography after extraction with Zwittergent 3–14. Sodium dodecyl sulfate-polyacrylamide gel electro-phoresis showed a relative molecular mass of 53 kDa for this protein with a pI of 6.3–6.8. Amino acid analysis revealed that this protein contained high proportions of hydrophobic amino acids (40.4%), and no cysteine could be detected. The N-terminus of the protein was blocked to Edman degradation. Rabbit antiserum raised against the purified 53 kDa protein reacted with the outer envelope of the T. denticola cell surface as confirmed by immunoelectron microscopy. This rabbit antiserum reacted with 4 of the 11 strains of treponemes tested in this study. Sera from 9 to 18 periodontitis patients reacted strongly with this 53 kDa cell envelope protein of T. denticola as determined by immunoblotting analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1994.tb01093.x
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    Paper (German National Licenses)
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