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Journal Abstract Search

251 related items for PubMed ID: 5003988

  • 1. Characterization of the reactive sulfhydryl groups in carbamyl phosphate synthetase of Escherichia coli.
    Foley R, Poon J, Anderson PM.
    Biochemistry; 1971 Nov 23; 10(24):4562-9. PubMed ID: 5003988
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  • 3. Evidence for the presence of two nonidentical subunits in carbamyl phosphate synthetase of Escherichia coli.
    Matthews SL, Anderson PM.
    Biochemistry; 1972 Mar 28; 11(7):1176-83. PubMed ID: 4552049
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  • 7. Half-of-the-sites reactivity and the conformational states of cytidine triphosphate synthetase.
    Levitzki A, Stallcup WB, Koshland DE.
    Biochemistry; 1971 Aug 31; 10(18):3371-8. PubMed ID: 4940762
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  • 8. Substrate-induced changes in reactivity of sulfhydryl groups of carbamyl phosphate synthetase.
    Novoa WB, Tigier HA, Grisolia S.
    Biochim Biophys Acta; 1966 Jan 11; 113(1):84-94. PubMed ID: 5940636
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  • 11. Carbamyl phosphate synthesis in a land snail, Strophocheilus oblongus.
    Tramell PR, Campbell JW.
    J Biol Chem; 1970 Dec 25; 245(24):6634-41. PubMed ID: 4320609
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  • 14. Reversible dissociation of the monomer of glutamine-dependent carbamyl phosphate synthetase into catalytically active heavy and light subunits.
    Trotta PP, Pinkus LM, Haschemeyer RH, Meister A.
    J Biol Chem; 1974 Jan 25; 249(2):492-9. PubMed ID: 4358555
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  • 17. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. 4. Isolation, molecular weight, amino acid analysis and behaviour of the sulfhydryl groups of the protein catalyzing the two activities.
    Truffa-Bachi P, Van Rapenbusch R, Janin J, Gros C, Cohen GN.
    Eur J Biochem; 1968 Jun 25; 5(1):73-80. PubMed ID: 4873312
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  • 18. IDENTITY IN ESCHERICHIA COLI OF CARBAMYL PHOSPHOKINASE AND AN ACTIVITY WHICH CATALYZES AMINO GROUP TRANSFER FROM GLUTAMINE TO ORNITHINE IN CITRULLINE SYNTHESIS.
    KALMAN SM, DUFFIELD PH, BRZOZOWSKI T.
    Biochem Biophys Res Commun; 1965 Feb 17; 18():530-7. PubMed ID: 14301456
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  • 19. Seryl transfer ribonucleic acid synthetase from Escherichia coli. Substrate binding and chemical modification of cysteinyl residues.
    Waterson RM, Clarke SJ, Kalousek F, Konigsberg WH.
    J Biol Chem; 1973 Jun 25; 248(12):4181-8. PubMed ID: 4576131
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  • 20. Nucleoside diphosphokinase from beef heart mitochondria. Purification and properties.
    Colomb MG, Chéruy A, Vignais PV.
    Biochemistry; 1969 May 25; 8(5):1926-39. PubMed ID: 5785215
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