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Journal Abstract Search

142 related items for PubMed ID: 4584821

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  • 5. A study of the sulfhydryl groups of the catalytic subunit of Escherichia coli aspartate transcarbamylase. The use of enzyme--5-thio-2-nitrobenzoate mixed disulfides as intermediates in modifying enzyme sulfhydryl groups.
    Vanaman TC, Stark GR.
    J Biol Chem; 1970 Jul 25; 245(14):3565-73. PubMed ID: 4919212
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  • 8. Interaction of aspartate transcarbamylase with 5-bromocytidine 5'-tri-, di-, and monophosphates.
    Tondre C, Hammes GG.
    Biochemistry; 1974 Jul 16; 13(15):3131-6. PubMed ID: 4601429
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  • 9. An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate.
    Matsumoto S, Hammes GG.
    Biochemistry; 1973 Mar 27; 12(7):1388-94. PubMed ID: 4572358
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  • 10. Conformational changes in aspartate trancarbamylase. I. Studies of ligand binding and of subunit interactions by circular dichroism spectroscopy.
    Griffin JH, Rosenbusch JP, Weber KK, Blout ER.
    J Biol Chem; 1972 Oct 25; 247(20):6482-90. PubMed ID: 4561937
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  • 13. The modification of the catalytic chain sulfhydryl group of aspartate transcarbamylase with mercurinitrophenols.
    Evans DR, Lipscomb WN.
    J Biol Chem; 1979 Nov 10; 254(21):10679-85. PubMed ID: 40972
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  • 15. A role for zinc in the quaternary structure of aspartate transcarbamylase from Escherichia coli.
    Nelbach ME, Pigiet VP, Gerhart JC, Schachman HK.
    Biochemistry; 1972 Feb 01; 11(3):315-27. PubMed ID: 4550953
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  • 16. Escherichia coli aspartate transcarbamylase: the relation between structure and function.
    Kantrowitz ER, Lipscomb WN.
    Science; 1988 Aug 05; 241(4866):669-74. PubMed ID: 3041592
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  • 19. Kinetic mechanism of catalytic subunits (c3) of E. coli aspartate transcarbamylase at pH 7.0.
    Hsuanyu Y, Wedler FC.
    Biochim Biophys Acta; 1988 Dec 02; 957(3):455-8. PubMed ID: 3058211
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