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  • 1980-1984  (2)
  • Analytical Chemistry and Spectroscopy  (1)
  • Pseudopseudohypoparathyroidism  (1)
  • Acidic uncoupler
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  • 1
    ISSN: 1432-1076
    Keywords: Pseudohypoparathyroidism ; Pseudopseudohypoparathyroidism ; 1,25-dihydroxyvitamin D
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In order to clarify the complex interrelationship between serum calcium, 1,25-dihydroxyvitamin D (1,25(OH)2D), and parathyroid hormone (PTH), and the urinary excretion of cyclic AMP (cAMP) in response to exogenous PTH in pseudohypoparathyroidism (PHP) and related diseases, we investigated 3 patients with parathyroid disorders before and after treatment with 1α-hydroxyvitamin D3 (1α-OH-D3). Low plasma 1,25(OH)2D before treatment increased after giving 1α-OH-D3 (0.1 μg/kg/day), where-as high plasma PTH measured by the C-terminal assay (C-PTH) decreased in all 3. No response in urinary cAMP was found before or after treatment in 2 patients with PHP type I, despite the fall of plasma C-PTH. However, in one patient with extremely high plasma C-PTH but normal N-PTH (measured by a homologous radioimmunoassay using 1–34 human PTH), urinary cAMP response to exogenous PTH was increased after treatment with 1α-OH-D3. We suggest that he had pseudopseudohypoparathyroidism (PPHP) with Albright's hereditary osteodystrophy and a partial deficiency of renal 1α-hydroxylase. In this patient secondary hyperparathyroidism is thought to be due to 1,25(OH)2D deficiency, and the decreased responsiveness to exogenous PTH before treatment due to excess PTH occupying renal receptors.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 8 (1981), S. 25-30 
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Field desorption mass spectra of tryptic peptides of normal human hemoglobin α-, β-, γ-, δ-chains and abnormal β-chain of hemoglobin S were studied. Almost all mass peaks of the protonated molecular ions of tryptic peptides and many doubly charged ions were observed. The molecular weights of all tryptic peptides were estimated from the mass spectra, the heaviest mass being m/z 2955, and coincided with the values obtained from the known amino acid sequences. The different chains of hemoglobin can be distinguished by their field desorption mass spectra. The mass spectrum of abnormal β-chain of hemoglobin S (sickle-cell-anemia) showed a shift of the characteristic line due to the mutation of amino acid.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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