GuHC1 induced unfolding-folding transition of a hinge-bending protein: horse muscle phosphoglycerate kinase |
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Authors: | M Desmadril A Mitraki J M Betton J M Yon |
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Institution: | Laboratoire d''Enzymologie Physico-Chimique et Moléculaire Bâtiment 430 - Groupe de Recherche du C.N.R.S. associé à l''Université de Paris-Sud, 91405 Orsay-France |
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Abstract: | The antineoplastic compound N2-methyl-9-hydroxyellipticinium (9-OH-NME) is able to bind to different biological molecules after an oxidative activation by horseradish peroxidase and hydrogen peroxide. In this study, the efficient covalent binding in vitro of 9-OH-NME onto RNA and poly A is described. The phenomenon is analyzed by different HPLC methods and the yield of binding is determined using 3H]9-OH-NME. For an initial ratio drug per nucleotide of 0.07, the rb obtained (ratio of drug bound per nucleotide) of 0.026 for RNA and 0.044 for poly A, which represent respectively a yield of 40% and 60% for the drug fixation onto these macromolecules. These facts demonstrate the high electrophilicity of para-quinone-imine derivatives in ellipticinium series. |
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Keywords: | Author to whom correspondence should be addressed |
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