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- W1976204266 abstract "Abstract The kinetic dissociation of Limulus oxyhemocyanin and apohemocyanin in alkaline pH have been studied using a high-performance liquid chromatographic method capable of measuring both the subunit and the aggregated proteins. The results show that the oxy- and apohemocyanins exhibit two distinct dissociation kinetics marked by their differences in aggregation patterns. For oxyhemocyanin, the kinetics occur at pH 7.8 and above and show a three-step dissociation of the 24-mer to the subunits. Each reaction step is characterized by the ionization of one set of protons with higher p K a associated with the dissociation of smaller aggregates. Binding of imidazole at or near the copper active site inhibits the dissociation kinetics. Cyanide ion, which removes the active copper from the protein, causes complete dissociation of the protein into subunits. For apohemocyanin, a two-step dissociation of the protein into subunits at pH 7.6 and above was observed. The kinetic results show a subunit ratio of 3:2 for the two aggregates, suggesting that the subunits of the copper-free protein may aggregate into dimers and trimers. In the pH range 6.5–7.5, apohemocyanin does not undergo kinetic dissociation. Since the protein has the highest state of aggregation at pH 6.5, association of the trimers into a larger aggregate such as a hexamer at this pH is also postulated." @default.
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- W1976204266 date "1990-04-01" @default.
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- W1976204266 title "Kinetic studies of the molecular aggregation of Limulus oxyhemocyanin and apohemocyanin" @default.
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- W1976204266 doi "https://doi.org/10.1016/0162-0134(90)80004-h" @default.
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