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  • 1975-1979  (3)
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Material
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Year
  • 1
    Electronic Resource
    Electronic Resource
    A MOUSE PLASMA SUBSTANCE CARRYING β2-MICROGLOBULIN ACTIVITY AND LACKING IN H-2 ALLOANTIGENIC ACTIVITY (1976)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 3 (1976), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A mouse plasma substance carrying β2-microglobulin activity and lacking in H-2 alloantigenic activity was separated from the blood plasma of A/J strain female mice. The plasma substance had a molecular size of about 300,000–400,000 daltons and an electrophoretic mobility of α-globulin. The plasma substance was split by papain digestion to a fragment of about 50,000–60,000 daltons that still carried β2-microglobulin activity. The papain-split plasma substance was devoid of H-2 alloantigenic activities and Thy-1 and TL alloantigenic activities as well, but yet had a two-component structure that was similar to papainsolubilized H-2 molecules. It contained a 37,000-dalton component linked non-covalently to an 11,000-dalton component, i.e. mouse β2-microglobulin. This plasma substance appears to be different from Ss protein or Slp protein, both found in mouse serum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1976.tb00563.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    THE COMPONENT FRAGMENTS OBTAINED BY ACID DISSOCIATION OF PAPAIN-SOLUBILIZED H-2 MOLECULES (1976)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 3 (1976), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: H-2Kk and H-2Dd molecules were specifically purified from a radioiodinated H-2a preparation obtained by papain digestion of spleen cell membranes of A/J strain mice. The molecules were isolated by binding to H-2 alloantisera of the corresponding private specificity followed by precipitation with rabbit anti-mouse IgG antiserum. The specifically precipitated radioiodinated H-2Kk and H-2Dd molecules were dissociated by acid treatment into large and small components of about 37,000 and 11,000 daltons respectively. These were separated by gel filtration at acid pH or by gel isoelectric focusing in the presence of 6 M urea. Each component separated by gel filtration of the acid-dissociated H-2 molecules showed a high degree of size homogeneity as determined by sodium dodecyl sulphate-acrylamide gel electrophoresis. Upon gel isoelectric focusing, however, the small components showed two peaks of radioactivity closely located together at pH 7–8, both of which had a restricted pH range, while the large components gave one peak of a relatively wide pH range of pH 5–6. The H-2Kk and H-2Dd molecules gave essentially the same pattern in terms of the numbers and the positions of the radioactivity bands. Under the iodination conditions used the large components of H-2Kk molecules contained more radioactivity than the small components, while the reverse was true in case of H-2Dd molecules. Such a difference was also found with H-2Kk and H-2Dd molecules isolated by use of alloantisera of the respective public specificity. The assay of binding of the isolated components with H-2 alloantisera of defined specificity revealed that the large components retain most of the allospecificities of the parental H-2 molecules. No H-2 allospecificities were found on the small components. The small components showed extensive binding with rabbit antiserum against mouse β2-microglobin. The same antiserum did not show any binding with the large components. On the other hand, both of the components did bind with rabbit antiserum against papain-solubilized H-2 molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1976.tb00554.x
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  • 3
    Electronic Resource
    Electronic Resource
    Reverse transcriptase of foamy virus (1977)
    Springer
    Archives of virology 55 (1977), S. 187-200 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Reverse transcriptase from foamy virus, strain H4188 was estimated and purified. The enzyme has the following characteristics: 1. The reaction utilized preferentially oligo (dT) poly (rA) as a primer-template; however, the synthetic primer-template oligo (dT) poly (dA) could also be used to some extent. 2. The reaction utilized oligo (dG) poly (rC) as a primer-template with very low efficiency. 3. The crude virus preparation had a detectable endogenous reaction using the four deoxyribonucleotides for DNA polymerization. 4. The cation requirement for the enzyme reaction was much more biased for Mn++ than for Mg++ ions. 5. The molecular weight of the partially-purified enzyme was estimated to be about 80,000. Aggregates of 240,000 daltons were also seen. The activity of this enzyme was not inhibited by antisera against the reverse transcriptases of various type C RNA viruses, namely, feline endogenous leukemia virus, RD 114, Woolly simian sarcoma virus (SSV-1) and avian myeloblastosis virus (AMV). Antiserum against Rauscher leukemia virus (RLV) enzyme was marginally active against foamy virus enzyme, perhaps indicating a slight cross-reaction. The biochemical characteristics of foamy virus reverse transcriptase seemed to be very close to those of the type C RNA viruses, but the immunological reaction proved that the foamy virus reverse transcriptase was distinct from the others.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01319905
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    Paper (German National Licenses)
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