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Sökning: db:Swepub > Linnéuniversitetet > (1975-1979)

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  • Brodelius, Peter, et al. (författare)
  • Determination of Dissociation Constants for Binary Dehydrogenase-Coenzyme Complexes by (Bio)Affinity Chromatography on an Immobilized AMP-Analogue
  • 1976
  • Ingår i: Analytical biochemistry. - : Elsevier BV. - 0003-2697. ; 72:1-2, s. 629-636
  • Tidskriftsartikel (refereegranskat)abstract
    • Various alcohol and lactate dehydrogenases were adsorbed to an affinity column of immobilized N6-(6-aminohexyl)-AMP and subsequently eluted with gradients of coenzymes or coenzyme fragments. A linear relation was observed between the eluting concentration of nucleotide and the reported dissociation constants for the corresponding binary enzyme-nucleotide complexes. This relation has been utilized to determine unknown dissociation constants by affinity chromatography. The method presented can also be utilized for the estimation of dissociation constants betweendehydrogenases and coenzyme analogues. 
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  • Brodelius, Peter, et al. (författare)
  • Studies of Bovine Liver Glutamate Dehydrogenase by Analytical Affinity Chromatography on Immobilized AMP Analogs
  • 1979
  • Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 194:2, s. 449-456
  • Tidskriftsartikel (refereegranskat)abstract
    • Bovine liver glutamate dehydrogenase has been studied by analytical affinity chromatography on two immobilized AMP analogs, i.e., N6-(6-aminohexyl)-AMP and 8-(6-aminohexyl)-amino-AMP. The existence of various enzyme-coenzyme and enzyme-effector complexes has been verified. Also the cooperative formation of two ternary complexes, i.e., glutamic dehydrogenase (GHD)-NADP-glutamate and GDH-ADP-leucine, has been shown. The results of this study have been rationalized by the “ligand exclusion theory.” which has been proposed for the regulation of the glutamic dehydrogenase. It has been shown that the active site and the ADP-binding effector site are oriented close to each other on the enzyme. Furthermore, the data suggest that the adenylic site is not identical to the nonactive coenzyme binding site. A mechanism based on electrostatic interactions is suggested for the cooperative binding of oxidized coenzyme and substrate. Dissociation constants for complexes between the enzyme and two coenzyme fragments (P-ADPR and 2′,5′-ADP) have been estimated.
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  • Brodelius, Peter, et al. (författare)
  • The Synthesis of 8-(6-Aminohexyl)-Amino-GMP and Its Applications as a General Ligand in Affinity Chromatography
  • 1978
  • Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 188:1, s. 228-231
  • Tidskriftsartikel (refereegranskat)abstract
    • The synthesis of a new general ligand, i.e., 8-(6-aminohexyl)-amino-GMP, has been achieved by bromination of GMP and subsequent substitution of the bromine for hexamethylene diamine. The overall yield of the synthesis has been 60 to 70%. This new general ligand was immobilized on BrN-activated Sepharose and used as an affinity adsorbent for inosinic acid dehydrogenase (E.C. 1.2.1.14) from Aerobacter aerogenes. Various elution methods were investigated in order to increase the specific activity of the purified enzyme. 
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