Theory of sedimentation for kinetically controlled dimerization reactions.
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Biomedical subjects
Publications and source records attributed to J R Cann.
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Ligand-mediated association-dissociation reactions can give rise to band sedimentation patterns showing bimodal bands despite instantaneous establishment of equilibrium. Weaker interactions result in unimodal bands whose sedimentation coefficients decrease with time of sedimentation and in characteristic patterns of total ligand. The implications of these results for fundamental investigations of protein interactions and for conventional analytical applications of zone sedimentation and molecular sieve chromatography are considered.
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Aromatic compounds like chlorpromazine and benzoate and its homologs strongly enhance the rate of heat denaturation of myoglobin. The latter apparently exert their action by complexing with a single kind of site in the hemeprotein. Both charge-transfer and hydrophobic interactions are implicated in complex formation, most probably with the heme moiety.
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