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  • 11
    Electronic Resource
    Electronic Resource
    FLUX RESTORATION OF REVERSE OSMOSIS MEMBRANES BY INTERMITTENT LATERAL SURFACE FLUSHING FOR ORANGE JUICE PROCESSING (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), 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: A newly developed method for washing membranes and the adhesive strength of mandarin orange juice fouling on reverse osmosis membranes were studied. When the permeation rate decreased, it was restored to more than 90% of its original value by a lateral surface flushing of highly accelerated mandarin orange juice driven by the expansion force of compressed gas. For runs of 4–5 hr duration with 10° Brix feed, the normal operating cycle was 45 min of reverse osmosis concentration followed by a 10-sec wash. Membranes treated at higher temperature have a more condensed surface from which deposits are easily removed. However, high axial flow rates, which are useful for preventing the fouling on the membrane, actually promote permanent fouling.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1978.tb02467.x
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  • 12
    Electronic Resource
    Electronic Resource
    Expression of tuna growth hormone cDNA in Escherichia coli (1989)
    Springer
    Applied microbiology and biotechnology 30 (1989), S. 153-159 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary In order to produce tuna (Thunnus thynnus) growth hormone (GH), expression plasmid (pUES13S) carrying tuna GH cDNA was constructed using a vector (pKK223-3), in which the replication origin was replaced with that of pUC19. The expression of the tuna GH cDNA was greatly affected by the distance between a Shine-Dalgarno (SD) sequence and the initiation codon (ATG) and was most efficient when the distance was adjusted to 13 base pairs (bp). The amount of tuna GH produced by Escherichia coli JM109 with pUES13S was more than 12.5% of the total cytosolic proteins and the product was immunologically identified to be tuna GH (mol. wt. 21 000) by Western blot analysis using tuna GH specific immunoglobulin G (IgG). Another plasmid (pUES13S-2) containing tandemly polymerized tuna GH cDNA was constructed, to improve the productivity of tuna GH. When E. coli JM109 carrying pUES13S-2 was incubated at 40°C, the amount of tuna GH produced reached about 20% of the total cytosolic proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264004
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  • 13
    Electronic Resource
    Electronic Resource
    Cloning and expression in Escherichia coliof the gene encoding the Proteus vulgaris chondroitin ABC lyase (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 39-46 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract. The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shine-Dalgarno ribosomal binding site. Promoter-like and ρ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G+C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, and has a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00166079
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  • 14
    Electronic Resource
    Electronic Resource
    Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 39-46 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00166079
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  • 15
    Electronic Resource
    Electronic Resource
    β 2 -Microglobulin restriction of antigen presentation (1990)
    [s.l.] : Nature Publishing Group
    Nature 346 (1990), S. 751-754 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] DBA/2 (H-2d, Β2ma) mice were immunized with P815 (H-2d, /32ma) mouse mastocytoma cells expressing the transfected mouse /32mb gene. Cloned cytotoxic T lymphocytes (LAZ CTLs) showing specific lytic activity towards P815 cells transfected with mouse /32m were isolated. Experiments were performed ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/346751a0
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  • 16
    Electronic Resource
    Electronic Resource
    Importance of GAD65 peptides and I-Ag7 in the development of insulitis in nonobese diabetic mice (2000)
    Springer
    Immunogenetics 51 (2000), S. 538-545 
    Details
    ISSN: 1432-1211
    Keywords: Key words NOD mouse ; GAD65 ; I-Ag7 ; Peptide ; Vaccine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Insulin-dependent diabetes mellitus (IDDM) develops in nonobese diabetic (NOD) mice through the destruction of the B cells in pancreatic Langerhans islets by islet autoantigen-specific T cells. The islet autoantigen glutamic acid decarboxylase 65 (GAD65) is thought to be a major target autoantigen in IDDM. In the present report, we established GAD65-specific T-cell clones using overlapping peptides that cover the amino acid sequences of mouse GAD65. T-cell epitopes of GAD65 were characterized by proliferation and binding assays using various analogue peptides and wild-type or mutant I-Ag7 transfectants. The efficacy of the peptide vaccine in IDDM was determined by administering T-cell epitope peptides to NOD mice and evaluating the histopathology of their insulitis. We obtained two types of T-cell clone, one specific for peptide p316–335 and another specific for p531–545 of GAD65. The p531–545 site has already been identified, but we report the p316–335 site for the first time. T-cell clones recognized those peptides in the wild-type I-Ag7 but not in the mutant I-Ag7 in which the serine at position 57 of the β-chain was replaced by an aspartic acid. Both the p316–335 and p531–545 peptides bound weakly to I-Ag7. Some peptides with amino acid substitutions had antagonistic activity, and administration of a large amount of wild-type peptide reduced the severity of insulitis in NOD mice. Our results suggest that peptide vaccine therapy may be useful in autoimmune diseases, including IDDM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510000173
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  • 17
    Electronic Resource
    Electronic Resource
    Tyrosinase epitope recognized by an HLA-DR-restricted T-cell line from a Vogt-Koyanagi-Harada disease patient (1998)
    Springer
    Immunogenetics 47 (1998), S. 398-403 
    Details
    ISSN: 1432-1211
    Keywords: Key words HLA ; Peptide ; VKH disease ; Tyrosinase ; T-cell response
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Human T-cell-mediated autoimmune diseases are often genetically linked to particular alleles of HLA class II genes. Vogt-Koyanagi-Harada’s (VKH) disease, which is regarded as an autoimmune disorder in multiple organs containing melanocytes, has been found to be associated with HLA-DR4 (DRB1*0405) and HLA-DR53 (DRB4*0101). Tyrosinase is a melanoma antigen (Ag) expressed by normal melanocytes as well as melanoma cells against which responses by autologous T cells have been detected. We established a T-cell line from the peripheral blood of a patient with VKH disease which responded to synthetic peptides corresponding to tyrosinase. The T-cell line was generated which recognized the tyrosinase p188 – 208 peptide when presented by the HLA-DR4 (DRB1*0405) molecule on the surface of HLA class II-expressing L-cell transfectants. The minimal antigenic peptide which induced T-cell responses was an 11-amino-acid sequence and located at tyrosinase p193 – 203 (E-I-W-R-D-I-D-F-A-H-E). This peptide contained the DRB1*0405-binding peptide motif (hydrophobic residues (Y, F, W) at position 1 as an anchor residue, and negatively charged residues (D, E) at position 9), which corresponded to the W at p195 and the D at p203. These observations demonstrate that tyrosinase peptides are immunogenic, and may be a candidate for an autoantigen in VKH disease, suggesting that probing the T-cell responses against synthetic peptides is a productive approach for identifying the autoantigenic peptides associated with autoimmune diseases including VKH disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510050375
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  • 18
    Electronic Resource
    Electronic Resource
    Evidence for two B-cell alloantigen loci in theHLA-D Region (1979)
    Springer
    Immunogenetics 9 (1979), S. 335-351 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Antigenic determinants recognizable by human antisera (Hon 7 and 2075abs sera) were found in a partially purified antigen preparation obtained from an HLA-D and -DR homozygous cell line (EBV-Wa). Sequential coprecipition tests showed that two determinants detectable with Hon 7 and 2075abs sera (Hon 7 and 2075abs determinants) were present on different molecules. These two antigenic determinants were shown to be allotypic and were expressed predominantly in the B-cell-rich fraction. Family studies showed that both antigenic determinants segregated concordantly with respectiveHLA haplotypes. In the population study, the 2075abs and Hon 7 determinants were shown to be in strong linkage disequilibrium and the 2075abs determinant perfectly correlated with the HLA-DRw4 specificity. The results indicate that the Hon 7 determinant is coded for by a gene distinct from alleles at theHLA-DR locus. Furthermore, the locus (Hon 7) coding for the Hon 7 determinant is suggested to be very closely linked with theHLA-DR locus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01570429
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  • 19
    Electronic Resource
    Electronic Resource
    New mouse immunoglobulin a heavy chain allotype specificities detected using the hybridoma-derived IgA of I/St Mice (1981)
    Springer
    Immunogenetics 13 (1981), S. 475-481 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Immunizations of C57BL/6 and A mice with IgA derived from the I/St mouse strain yield alloantisera which detect two allotypic determinants of immunoglobulin A. The two determinants display discrete strain distributions. The first, identified by the alloantiserum C57BL/6 anti-IgA of I/St strain hybridoma ID150, follows the Igh c haplotype, and the second, identified by the alloantiserum A anti-IgA of I/St strain hybridoma ID150, correlates with Igh c and Igh c haplotypes. Absorption with monoclonal IgM, which has the same idiotype as the ID150 IgA clone, removed idiotype-specific antibodies from both alloantisera. The remaining antibodies are directed against determinants associated with the α chain constant region, as shown by absorption with monoclonal IgA. By use of recombinant inbred strains of mice and mice congenic at the Igh locus, the loci controlling both Cα allotypic determinants have been mapped to the Igh region on chromosome 12.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00343715
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  • 20
    Electronic Resource
    Electronic Resource
    Ly-m19: The Lyb-2 region of mouse chromosome 4 controls a new surface alloantigen (1981)
    Springer
    Immunogenetics 13 (1981), S. 539-546 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Spleen cells from an SJL mouse immunized with 70'/3 cells, an established pre-B cell line, were fused with cells of the nonsecretor myeloma line NS.1. One established hybridoma cell line (clone K10.6) continuously secreted antibody that recognized a new antigenic specificity tentatively named Ly-m19. This newly found antigen is detectable on both T and B cells. Cytotoxicity assays reveal that 75 percent of the spleen and lymph-node cells, 35 percent of bone-marrow cells, and 15 percent of thymus cells reacted with antibody of clone K10.6. Strains expressing the specificity Ly-m19.1 are characterized by negative reactions and include the strains AKR, CE/J, RF/J, GR/A, SJL, P/J, BDP/J, and LG/J. All other strains so far tested are Ly-m19.2. This strain distribution pattern distinguishes Ly-m19 from any known murine lymphocyte alloantigen, but it parallels the Lyb-2 c haplotype. Linkage test of a set of AKXL recombinant inbred strains revealed close linkage of Ly-m19 and Lyb-2 loci on mouse chromosome 4.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00343721
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