大分子ACTHの性状に関する研究

概要

論文の詳細を見る
Crude ACTH preparation (Cortrophine) was selected as the starting material for the present studies. Crude ACTH preparation was subjected to gel filtration at 4°C on a Bio-Gel P-10 column of 1.5 × 85 cm. The column was eluted with 0.1N acetic acid, and 3 ml eluates were collected. Immunoreactive ACTH contents in each fraction were determined by radio-immunoassay. Bioassay was performed using isolated rat adrenal cells. On gel filtration, several immunoreactive and bioactive ACTH components were separated. These peaks were arbitrarily designated Fraction A and C. Fraction A emerged earliest, hence was assumed as having a larger molecular size. Fraction C was eluted at a position closely corresponding to that of authentic porcine ACTH. When Fraction A and C were refractionated on the same column, both of them emerged as homogenous peaks with no shift in their respective elution patterns. The immunoreactivity of Fraction A and C after refractionation were tested with an antiporcine ACTH antibody. Fraction C was found to have close immunologic similarity with authentic ACTH, where Fraction A seemed to have somewhat different immunor-reactivity. There was reasonable agreement between the biologic and immunologic potencies of Fraction C, when assayed using authentic or synthetic ACTH as a standard. <BR>In contrast, the biological activity of Fraction A was less than 1% of the activity as measured by radioimmunoassay. The biological activity of Fraction A, however, was not negligible, since it was clearly demonstrable when a considerable amount of it was subjected to the assay using isolated rat adrenal cells.
日本内分泌学会の論文

大分子ACTHの性状に関する研究

スポンサーリンク

概要

著者

関連論文

スポンサーリンク