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  • 1
    Electronic Resource
    Electronic Resource
    Primate relaxin: Synthesis of gorilla and rhesus monkey relaxins (1994)
    Springer
    The protein journal 13 (1994), S. 315-321 
    Details
    ISSN: 1573-4943
    Keywords: Solid-phase peptide synthesis ; gorilla relaxin ; rhesus monkey relaxin ; isolated rat heart chronotropic and inotropic assay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The synthesis of the hormone relaxin from the speciesGorilla gorilla (gorilla) andMacaca mulatta (rhesus monkey) has been achieved. Each of the two chains which constitute the peptide structures was assembled separately, the A-chains (24 amino acids) by the Boc-polystyrene solid-phase procedure and the B-chains (29 and 28 amino acids) by the Fmoc-polyamide (gorilla) and the Boc-polystyrene (rhesus monkey) solid-phase methods. After cleavage from the solid supports, the separate chains were purified to a high degree of homogeneity. Oxidative combination of the respective A- and B-chains in solution at highpH afforded the synthetic relaxins in low overall yield. Chemical and physiochemical characterization of the products confirmed both their purity and their conformational similarity to the human hormone. The synthetic gorilla and rhesus monkey relaxins were both found to possess potent chronotropic and inotropic activity in the isolated rat cardiac atrium assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01901564
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A test for prorelaxin-processing enzymes using unmodified peptide substrates (1995)
    Springer
    International journal of peptide research and therapeutics 2 (1995), S. 83-92 
    Details
    ISSN: 1573-3904
    Keywords: Relaxin ; Prohormone processing ; Endoproteolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Relaxin is a member of the insulin family of proteins. It is produced principally in ovarian cells by processing of its larger precursor, prorelaxin. The enzymes responsible for conversion of prorelaxin to the mature hormone have not yet been elucidated. A rapid and convenient test has been developed to detect prorelaxin-processing enzymes in porcine ovary extracts. Unmodified peptide substrates, which represent the two prorelaxin-processing sites, were chemically synthesised and nanomolar amounts of these substrates were incubated in solution with enzyme preparations. The resultant fragments were resolved using high performance liquid chromatography or capillary electrophoresis and identified by their retention times compared with synthetic standards. This test has been successfully used to identify and characterise a candidate prorelaxin-processing enzyme from chromatographically fractionated porcine ovary extracts. The enzyme was found to be a serine protease with preference for cleavage after tetrabasic sequences and with optimal activity at pH 5.5–6.5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00128502
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    Paper (German National Licenses)
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