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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 37 (1994), S. 436-438 
    ISSN: 1432-0428
    Keywords: Amylin physiology ; insulin secretion ; amylin antagonists ; islet paracrine physiology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To assess the effect of naturally-present amylin in the control of insulin release we infused a novel amylin antagonist, its 8–37 fragment, or amylin in anaesthetized rats for 60 min, and 30 min after the start arginine was infused for 14 min. Amylin8–37 decreased the blood glucose concentration by 18 % whereas the plasma insulin concentration was 90 % higher following arginine treatment. In contrast amylin infusion raised both glucose and insulin concentrations. These results suggest that while amylin added at high dose can induce peripheral insulin resistance, naturally present amylin tonally controls insulin secretion.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 37 (1994), S. 436-438 
    ISSN: 1432-0428
    Keywords: Key words Amylin physiology, insulin secretion, amylin antagonists, islet paracrine physiology.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To assess the effect of naturally-present amylin in the control of insulin release we infused a novel amylin antagonist, its 8–37 fragment, or amylin in anaesthetized rats for 60 min, and 30 min after the start arginine was infused for 14 min. Amylin8–37 decreased the blood glucose concentration by 18 % whereas the plasma insulin concentration was 90 % higher following arginine treatment. In contrast amylin infusion raised both glucose and insulin concentrations. These results suggest that while amylin added at high dose can induce peripheral insulin resistance, naturally present amylin tonally controls insulin secretion. [Diabetologia (1994) 37: 436–438]
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 2 (1968), S. 17-17 
    ISSN: 1432-0827
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 244 (1973), S. 438-440 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fraser and Kodicek9, however, in apparent support of this role of parathyroid hormone, recently showed convincingly that removal of the parathyroid and ultimobranchial glands in chicks almost abolished the production of 1,25-DHCC. We have fully confirmed these results but show here that they were ...
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 220 (1968), S. 984-986 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Two calcitonin peptides have been characterized from human C-cell tumours. This has important practical ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 297 (1982), S. 520-520 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] AFFINITY chromatography has marched out of the research laboratory and into the world. That was to be the message of the symposium held in June of last year at Veldhoven, of which this book is a record, and the organizers emphasized it by bringing together similar numbers of participants from ...
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  • 7
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 14162-14169 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 51 (1968), S. 1738-1742 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Two highly active calcitonin peptides, M with 32 amino acids, and D a dimer of M, were isolated from a large human mediastinal C cell tumour. D can easily be transformed into M by the action of 1N ammonia; D and M afford two different sulphoxides, but all four peptides yield the same product upon oxidation with performic acid. Both D and M have a potency of about 120 MRC units/mg dry weight; their sulphoxides, by contrast, are almost inactive. Tryptic digestion of M produces an N-terminal octadecapeptide (TrI) and a C-terminal tetradecapeptide (TrII), the latter being also obtained from D. Amino acid analysis and other analytical data are presented. The structure of the human calcitonin peptides D and M is thus very different from that of porcine α-thyrocalcitonin.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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