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Heme-peptide/protein Interactions: The Binding Of Heme Octa And Undecapeptides, And Microperoxidase-8 And -11, To Human Serum Albumin.

Paul A. Adams, R. Goold, A. Thumser
Published 1989 · Chemistry, Medicine

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The interaction of the heme octa (MP-8) and undeca (MP-11) peptides derived from cytochrome c with lipidated human serum albumin (HSA) has been investigated in aqueous solution. It is demonstrated that complex formation occurs in each case with a 1:1 stoichiometry. CN- binding has been used to investigate the accessibility of the heme in each complex by comparison with CN- interaction with methemalbumin. A preliminary study of the kinetics of the Fe3+MP-8/11 human serumalbumin (HSA) interaction demonstrates a clear ligand-size-related effect on mechanism of interaction--an ad hoc explanation of which is given in terms of HSA existing as two nonconverting conformers in solution.
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This paper is referenced by
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