Light-scattering Studies of the Interaction of Sodium Chondroitin Sulfate C with Bovine Serum Albumin
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概要
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Angular light-scattering investigations were carried out in 0.01 M sodium chloride solutions at 25°C for various mixed solutions of bovine serum albumin (BSA) and chondroitin sulfate (Chs). The experimental values of molecular weight and of the molecular dimensions showed an entirely different tendency from the calculated values, and we may assume that there is no interaction between them. It has, therefore, been concluded that Chs interacts with BSA strongly and that a complex is formed between them. For the soluble complex thus formed, the number of the bound BSA molecules with one Chs molecule was expressed by a Langmuir-type equation as a function of the amount of excess BSA existing free in the solution. When the latter was sufficiently large, the number of bound BSA molecules per Chs molecule approached 20.6.<BR>A Zimm plot of the complex was drawn, and the molecular weight, the radius of gyration, and the second virial coefficient of the complex were determined. It has been concluded from these results that the complex molecule has a long-like shape; the length was about 30% longer, but the diameter was about 6 times thicker, than the Chs molecule at the maximum binding of BSA.
- 公益社団法人 日本化学会の論文
著者
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Nakagaki Masayuki
Faculty of Living Science Osaka City University
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Sano Yoh
Faculty of Pharmaceutical Sciences, Kyoto University
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