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  • 1
    ISSN: 1573-4978
    Keywords: cDNA cloning ; gene structure ; Northern blot ; RalGDS ; variant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract RalGDS is a guanine nucleotide dissociation stimulator for Ral, which is a member of the Ras GTPase superfamily that regulates cellular proliferation, differentiation and transformation by mediating multiple signal transduction pathways. RalGDS can specifically promote the conversion from an inactive GDP-bound state to an active GTP-bound state for Ral. The cDNA of human RalGDS has been cloned recently. In this paper, by comparison between the gene's genomic and cDNA seqence, we determined the structure of the gene, which showed that the reported human RalGDS transcribed from 18 exons. Furthermore, a novel variant of RalGDS that codes for a protein with a different N-terminus was cloned and identified. Northern hybridization revealed that the novel transcript was of 6.0 kb in length while the transcript previously reported is of 4.0 kb. Both transcripts were ubiquitously expressed in human adult tissues examined, albeit with different amounts. In addition, this novel transcript was proved to be caused by employment of a new exon, designated as exon 1a, instead of the one, designated as exon 1b, in the reported cDNA. Thus, the RalGDS gene consists of at least 19 exons and spanned a 44 kb region. The length between exon 1a and exon 2 was 33 kb, while the length between exon 1b and exon 2 was 8.8 kb.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4978
    Keywords: cDNA cloning ; chromosome 3q25–26.2 ; gene structure ; human latexin ; Northern hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Latexin, a carboxypeptidase A inhibitor, is expressed in a cell type-specific manner in both central and peripheral nervous systems in the rat. It is used as a molecular marker for the regional specification of the neocortex. In this study, a cDNA was isolated from a human fetal brain cDNA library. The cDNA (LXN) contains an open reading frame encoding 222 amino acids. The comparison between the deduced amino acid sequences of LXN and latexins of rat and mouse revealed high sequence identity (84.2 and 84.7%, respectively). Northern blot analysis showed that LXN was expressed as a transcript of 1.3 kb in 15 out of 16 tissues examined, except in peripheral blood leukocyte. The expression levels were high in heart, prostate, ovary, kidney, pancreas, and colon, moderate or low in other tissues including brain. It is noteworthy that the tissue distribution of human LXN differs greatly to that of its homologue in the model animal, rat latexin. In addition, the LXN gene contains at least 6 exons and spans 5.9 kb according to the genomic sequence of the clone RP11-79M21 and the gap sequence cloned in this paper. LXN was assigned to 3q25-q26.2 according to the position of the marker SHGC-35682 found adjacent to LXN gene.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4927
    Keywords: HUMAN NEURONAL PROTEIN 17.3 ; MOUSE NP15.6 ; CDNA CLONING ; TISSUE EXPRESSIONAL ; CHARACTERIZATION
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A full-length cDNA of 595 bp was isolated froma human fetal brain cDNA library. It contains an openreading frame encoding 153 amino acids, with an 18-bp5′UTR and a 118-bp 3′UTR in which there isan atypicalpolyadenylation signal (ATTAAA). The calculatedmolecular weight of the deduced protein is 17.3 kU. Thepredicted isoelectric point is 4.89. On account of itshigh homology to mouse neuronal protein NP15.6(81.2% identity), the deduced protein was namedneuronal protein 17.3 (NP17.3). When its secondarystructure was examined by the GGBSM program of PCGENEsoftware, it was found that 32.6 and 15.0% of itsamino acids are involved in formingalpha-helices and beta-sheets, respectively. Examinedwith the PESTFIND program, a typical PEST region foundin rapidly degraded proteins was found between residue48and residue 68.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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