尿蛋白質の研究(第2報)
Bence-Jones蛋白尿の熱変性に関する超遠心分析による検討
1973 年 17 巻 2 号 p. 77-80
詳細
1973 年 17 巻 2 号 p. 77-80
Although Bence-Jones proteins are characterized by the property of precipitating on heating at 44-60°C and of redissolving on boiling, the factors governing this unusual solubility behavior have never been defined quantitatively, nor has the phenomenon been satisfactorily explained.
Measurements of the property of precipitating phenomena at high temperatures have been performed by Putnam with various optical instruments.
An ultracentrifugal study of the molecular size and shape changes occurring in Bence-Jones proteins in the temperatures ranging 30-100°C has become possible only with a reliable high temperature accessory to the analytical ultracentrifuge. This report describes the ultracentrifugal analysis of heat denaturations of Bence-Jones protein in solution at 30-100°C. The results obtained are as follows.
1) The Bence-Jones protein forms unstable rapidly sedimenting boundaries above a critical temperature of 60°C, and the sedimentation coefficient could not be obtained.
2) Molecular aggregation occurred when the solution of Bence-Jones protein was heated above 60°C and various types of aggregation products were suspected.
3) The method was found to be not satisfactory for the study of heat denaturation of the urmary Bence-Jones protein in this temperature range.
4) The technical problems associated with this study were discusssed.
