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  • 1
    Digitale Medien
    Digitale Medien
    Determination of plasma catecholamines by means of radioenzymatic labelling and high pressure liquid chromatographic separation (1981)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 315 (1981), S. 233-239 
    Details
    ISSN: 1432-1912
    Schlagwort(e): Plasma catecholamines ; HPLC separation ; Enzymatic labelling ; Performance characteristics ; Comparison of methods
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary 0.05 ml plasma samples are incubated with 3H-S-adenosylmethionine and catechol-O-methyl-transferase. The resulting methoxy derivatives are extracted, the extracts separated by high pressure liquid chromatography and the metanephrine fractions collected. Evaluation is performed by liquid scintillation counting of radioactivity in the respective fractions. The following performance criteria are presented: precision, accuracy, detectability (40 pg/ml for adrenaline and noradrenaline, 130 pg/ml for dopamine), linearity and day-by-day variation. Comparison with a standard method shows an excellent correlation for adrenaline and noradrenaline.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00499840
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Overexpression of Gsα subunit in thyroid tumors bearing a mutated Gsα gene (1995)
    Springer
    Journal of cancer research and clinical oncology 121 (1995), S. 219-224 
    Details
    ISSN: 1432-1335
    Schlagwort(e): Gsα gene ; Expression ; Point mutation ; Immunoblotting ; Thyroid tumors
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Point mutations occurring at codon 201 of the gene coding for the α subunit of the stimulatory G protein impair intrinsic GTPase activity and lead to a constitutive activation of adenylate cyclase. We have examined thyroid follicular and papillary carcinomas and follicular adenomas and found samples that bear this mutation at codon 201 of the Gsα gene. Both mutation-positive and mutation-negative tissue samples were investigated for the level of Gsα expression relative to a pool of normal thyroid tissue, using immunoblotting against two (mid-region-specific and C-end-specific) antipeptide antibodies. Using 8000g and 100 000g membrane fractions of homogenized tissues we have demonstrated that the Gsα proteins in normal ad neoplastic thyroid tissues are represented by three isoforms: 43 kDa, 45 kDa and 52 kDa. We have quantified and compared the amount of Gsα protein and find it is overexpressed in mutation-bearing tissue samples.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01366965
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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