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  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide (1996)
    Springer
    The protein journal 15 (1996), S. 345-350 
    Details
    ISSN: 1573-4943
    Keywords: Alkaline phosphatase ; inhibition ; chemical modification ; N-bromosuccinimide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The inactivation of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide has been studied using the kinetic method of the substrate reaction during modification of enzyme activity previously described by Tsou [(1988),Adv. Enzymol. Related Areas Mol. Biol. 61, 381–436]. The results show that inactivation of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined. Comparison of these rate constants indicates that the presence of substrate offers marked protection of this enzyme against inactivation by N-bromosuccinimide. The above results suggest that the tryptophan residue is essential for activity and is situated at the active site of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886860
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Intrinsic specificity of Ca2+-protein binding sites (1993)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 28 (1993), S. 1596-1601 
    Details
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The gas-phase chemistry of anionic [M + Cat2+ - 3H]- complexes between Ca2+-specific peptides and the alkaline earth metal ions Mg2+, Ca2+ and Ba2+ is reported. The metal ion complexes were studied using fast atom bombardment, collision-induced decomposition (CID) and molecular mechanical calculations. The CID reactions and molecular mechanical calculations revealed that the Ca2+-peptide complexes are bound differently to the Mg2+- and Ba2+-peptide complexes and that the intrinsic (gas-phase) chemistry is reflected by known aqueousphase chemistry.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/oms.1210281235
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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