Binding of alkylisocyanides with soybean leghemoglobin. Comparisons with sperm whale myoglobin.
作者： F. Stetzkowski , R. Cassoly , R. Banerjee
DOI: 10.1016/S0021-9258(19)86492-X
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摘要: The binding of various linear and branched chain alkylisocyanides to soybean leghemoglobin has been studied with respect association dissociation kinetics the results compared those obtained in parallel on sperm whale horse heart myoglobins; ligands used (methyl n-heptyl) cover a greater distribution lengths than hitherto used. rate constants are much higher for myoglobin, while rates slower. For given protein, not different when isocyanides (except methyl), whereas show complex behavior relation alkyl length; singular differences observed between myoglobin this regard. decrease from methyl n-propyl, but remain approximately same ligand carries still longer chain. In contrast, leghemoglobin, although they progressive important rise substituents: n-butyl n-pentyl.
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