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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Immunogenetics 8 (1979), S. 517-528 
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A variety of cytotoxic alloantisera directed against murine cell surface components were analyzed for their content of specific IgG1, IgG2a, and IgG2b antibodies by radioimmunoassay, and specific IgM antibodies by 2-mercaptoethanol inhibition of cytotoxicity. Results indicate: (1) that the IgM and IgG subclass content of specific antibodies in anti-Lyt antisera produced at M.I.T. and Sloan-Kettering using the same donor and recipient strains are similar; (2) that specific antibodies produced concurrently in the same mice against at least two different alloantigens (Lyt-3.1 and H-2k) can differ in IgG subclass content; and (3) that preparation of alloantisera against a given antigen (Lyt-3.1) using different combinations of donor and recipient strains can yield specific antibodies which differ in IgG subclass and cytotoxic IgM content. Thus, it appears that humoral immune responses to cell surface alloantigens are not random, but reflect both the antigens being recognized and the strains employed for the immunization.
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  • 6
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The Lyt-2 aallele of the C.AKR strain of mice (genotype Lyt-2 a, Lyt-3 a) was cloned, and its complete nucleotide sequence as well as that of 2 kb of 5′ flanking DNA was determined. The sequence was comapred with the partial sequence of the Lyt-2 aallele of DBA/2 (genotype Lyt-2 a, Lyt-3 b) and the nearly complete sequence of the B10.CAS2 Lyt-2 ballele reported by Liaw and coworkers (1986). The coding regions of the two Lyt-2 aalleles differ from each other by two nucleotide substitutions in the three exons over which they could be compared, resulting in two amino acid substitutions in the leader and transmembrane segments. The coding region of the C.AKR Lyt-2 aallele differs from the Lyt-2 ballele by two nucleotide substitutions in the extracellular V-like domain, one of which is silent and the second of which leads to substitution of valine for methionine at amino acid position 78 giving rise to the Lyt-2.1 allotypic specificity. The coding region of the DBA/2 Lyt-2 aallele shares with C.AKR the allotypic substitution at position 78 and differs from Lyt-2 bby three additional nucleotide substitutions in the coding regions, two of which lead to amino acid substitutions in the leader and transmembrane segments. It would therefore appear that the Lyt-2 alleles of the three strains analyzed are distinct, and the nomenclature Lyt-2 a1 and Lyt-2 a2 is suggested to distinguish the alleles of C.AKR and DBA/2, respectively. These alleles share a common difference from the Lyt-2 bgene product at position 78, and since the amino acid substitutions which distinguish them from each other are in the leader and transmembrane segments, their mature Lyt-2 gene products appear antigenically identical.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Immunogenetics 28 (1988), S. 353-361 
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The mouse Lyt-3 agene, which encodes the Lyt-3.1 T-cell surface alloantigen of the C.AKR strain, has been cloned, and the nucleotide sequence of its exons and more than 2 kb of 5′ flanking sequence have been determined. The gene extends over approximately 16 kb of DNA and consists of six exons encoding leader, leader plus V-like domain, membrane-proximal, transmembrane, and cytoplasmic domains. The only difference between the coding region of the Lyt-3 agene and the cDNA sequences reported for Lyt-3 b(Nakauchi et al. 1987, Panaccio et al. 1987) is at position 77 of the mature protein where Lyt-3 aencodes serine and Lyt-3 bencodes arginine. This substitution must therefore be the basis for the serological distinction between the Lyt-3.1 and Lyt-3.2 alloantigens. Potential TATA and CAAT sequences, two Sp1 protein binding sites, two extended repeats of the dinucleotide, CA, a number of short inverted repeats, and an inverted segment of the mouse B1 repetitive sequence are found 5′ to the Lyt-3 agene. Two consensus poly-A addition signals and a complete copy of the mouse B1 sequence are found 3′ to the gene. Both B1-related regions are flanked by short direct repeats suggesting that they arose by an insertional mechanism. Cotransfection of the Lyt-3 agene together with a cloned Lyt-2 agene resulted in expression of both Lyt-2 and Lyt-3.1 on the surface of Ltk− and BW5147 cells. Transfection of the Lyt-3 agene without Lyt-2 aled to expression of Lyt-3-related cellular RNA but did not result in surface expression of Lyt-3.1, suggesting that the Lyt-3 glycoprotein is not expressed on the cell surface in the absence of Lyt-2.
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  • 8
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The mouseIgK-VSer gene encodes an immunoglobulin κ light chain variable region which gives rise to two phenotypic polymorphisms of mouse κ chains. The nucleotide sequences of coding and flanking regions of theIgk-VSer c andIgk-VSer d alleles found in recently inbred strains of wild mice are compared with those of theIgk-VSer a andIgk-VSer b alleles described previously. Results suggest that the gene is evolving randomly and that framework 2 and complentarity determining region 2 are preserved, presumably for overall light chain structure. Results indicate that all four allels have an octamer motif upstream of the gene which should be functional and allow prediction of whether or not the product of the germ line gene will be detectable as either the IB-peptide or Ef1a phenotypic polymorphism. Southern hybridization of genomic DNA using as probe a 1-kbXba I-Xba I fragment located approximately 4 kb upstream of the BALB/cIgk-VSer b coding region demonstrated the presence of homologous DNA in mice bearing theIgk-VSer a allele and absence from mice bearing theIgk-VSer c andIgk-VSer d alleles. Nucleotide sequence comparison of BALB/c and SK/CamRk (Igk-VSer d ) DNA in this region demonstrated that BALB/c contained an insertion 2.4 kb in length which was absent from SK/CamRk. Both strains contain DNA homologous to the reverse complement of the mouse Bam5 repetitive element at the point of the insertion, with BALB/c containing approximately 70 nucleotides more of the element than SK/CamRk. Surprisingly, the strains containing DNA related to theXba I-Xba I probe are not those determined to be the most similar by nucleotide sequence comparisons and by the Phylogenetic Analysis Using Parsimony program. The evolutionary relationship of the alleles and a possible basis for the inconsistency presented by theXba I-Xba I fragment-related DNA are discussed.
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  • 9
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The Igk-J locus of the mouse encodes the immunoglobulin κ light chain joining (J) segments. Four Igk-J alleles have been described on the basis of restriction enzyme length polymorphisms. The nucleotide sequences of the Igk-J a allele (type strain, C.C58), Igk-J c allele (type strain, SJL/J), and Igk-J d allele (type strain, SK/CamRk) have been determined and are compared with the previously reported Igk-J b allele sequence (type strain, BALB/c). The mouse sequences are also compared with published sequences for rat and human J k sequences. Far more differences were found between the Igk-J a allele and the other mouse alleles than between any two of the latter. These result in two amino acid substitutions which distinguish the J2 and J3 1 segments of the Igk-J a allele from the other three alleles. Use of the Phylogenetic Analysis Using Parsimony program to generate a phylogenetic tree strongly indicates that after divergence from the rat ancestor, there appears to have been an early split between the Igk-J a allele and the evolutionary precursor of the other mouse alleles. There also appears to have been far less divergence from the ancestral condition in the Igk-J a allele than in the other alleles. Also, the presence of only one convergent mutation among the four mouse alleles provides strong evidence against any crossing over within the Igk-J locus during the history of these alleles. Finally, the differences in rates of evolution of the Igk-J alleles are in marked contrast to the relatively uniform rates of divergence of four alleles of a mouse V k gene, Igk-VSer.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Immunogenetics 7 (1978), S. 165-168 
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
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