J. Biochem, 1982, Vol. 91, No. 4 1267-1272
© 1982 Japanese Biochemical Society
research-article |
The Process of Dissolving Apolipoprotein A-I in an Aqueous Buffer1
Department of Etiology and Pathophysiology, National Cardiovascular Center Research Institute Suita, Osaka 565
Human plasma apolipoprotein A-I (apoA-I) has been studied in an aqueous solution by the techniques of high performance liquid chromatography (HPLC), circular dichroic spectroscopy, and sedimentation equilibrium ultracentrifugation. The results indicate that an oligomer is formed as an intermediate step of dissolving lyophilized apoA-I. The process of further dissolution of this oligomer is an irreversible, temperature-dependent dissociation. The half-life of this intermediate oligomer is 3 min at 37°C and 80 h at 30°C. The completely dissolved apoA-I in an aqueous buffer self-associates with conformational alteration. The self-association equilibrium is too rapid to be demonstrated by HPLC.
1This work was supported in part by a Grant-in-Aid for Scientific Research No. 448387, and by a Grant-in-Aid for Encouragement of Young Scientists No. 56790137 (ST) from the Ministry of Education, Science and Culture of Japan.
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