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Journal Abstract Search

146 related items for PubMed ID: 782521

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  • 7. Formamide-induced dissociation and inactivation of Escherichia coli alkaline phosphatase. Metal-dependent reassociation and restoration of activity from isolated subunits.
    Falk MC, Bethune JL, Vallee BL.
    Biochemistry; 1982 Mar 30; 21(7):1471-8. PubMed ID: 7044413
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  • 8. Role of metal ions in Escherichia coli alkaline phosphatase. A study of the metal-water interaction by nuclear relaxation rate measurements on water protons.
    Zukin RS, Hollis DP.
    J Biol Chem; 1975 Feb 10; 250(3):835-42. PubMed ID: 163241
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  • 9. Fluorescence properties of terbium-alkaline phosphatase.
    Sherry AD, Au-Young S, Cottam GL.
    Arch Biochem Biophys; 1978 Aug 10; 189(2):277-82. PubMed ID: 360992
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  • 13. 31 P NMR studies on phosphate binding to the Zn 2+ , Co 2+ and Mn 2+ forms of escherichia coli alkaline phosphatase.
    Csopak H, Drakenberg T.
    FEBS Lett; 1973 Mar 15; 30(3):296-300. PubMed ID: 4573438
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  • 14. Hydrogen-tritium exchange of partially and fully reconstituted zinc and cobalt alkaline phosphatase of Escherichia coli.
    Brown EM, Ulmer DD, Vallee BL.
    Biochemistry; 1974 Dec 17; 13(26):5328-34. PubMed ID: 4611482
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  • 15. Role of metal ions in the reaction catalyzed by L-ribulose-5-phosphate 4-epimerase.
    Lee LV, Poyner RR, Vu MV, Cleland WW.
    Biochemistry; 2000 Apr 25; 39(16):4821-30. PubMed ID: 10769139
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  • 16. Magnetic circular dichroic spectra of cobalt(II) substituted metalloenzymes.
    Holmquist B, Kaden TA, Vallee BL.
    Biochemistry; 1975 Apr 08; 14(7):1454-61. PubMed ID: 235952
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  • 17. Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphatase.
    Murphy JE, Xu X, Kantrowitz ER.
    J Biol Chem; 1993 Oct 15; 268(29):21497-500. PubMed ID: 8407998
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  • 20. Trypsin-modified alkaline phosphatase. Formation of apoenzyme monomer and hybrid dimer.
    Roberts CH, Chlebowski JF.
    J Biol Chem; 1985 Jun 25; 260(12):7557-61. PubMed ID: 3889000
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