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- W1983271599 abstract "Previous studies of the interaction of the haem undecapeptide (MP-11) with lipidated human serum albumin in aqueous solution have been extended to a range of MeOH/H2O solution compositions. It is demonstrated that the kinetic mechanism for the interaction does not change from a simple second- and first-order reversible scheme as XMeOH is increased, however while k1 - the association rate constant is essentially invariant with XMeOH, k−1 increases some 600-fold over the range studied. The result is interpreted in terms of increased solvational stabilization of MP-11 and transition state as XMeOH increases and it is noted that the system provides a simple demonstration of the effect of hydrophobicity on facilitating transported ligand release from ligand/carrier protein molecules." @default.
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- W1983271599 date "1993-04-01" @default.
- W1983271599 modified "2023-09-24" @default.
- W1983271599 title "Haem-peptide-protein interactions: Part 5. The haem undecapeptide microperoxidase-11 (Fe3+MP-11)/human serum albumin (HSA) reaction in aqueous methanolic solution. A simple system demonstrating the effect of hydrophobicity on ligand release from a ligand-protein complex" @default.
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- W1983271599 doi "https://doi.org/10.1016/0162-0134(93)80009-x" @default.
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