人胎盤性Immunoreactive ACTHに関する研究:(1) 人満期胎盤中の大分子Immunoreactive ACTHの検出

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Extracts of human term placenta were fractionated by Sephadex G-75 gel filtration and assayed for immunoreactive ACTH. Both high and low molecular weight protein fractions were detected to be immunologically reactive toward anti-human ACTH (1-39α) antibody. For the extraction of low molecular weight ACTH from human term placenta (pl. -ACTH), a glacial acetic acid-acetone mixture was employed, while a pH 3.0-HCl solution was used for high molecular weight immunoreactive ACTH.<BR>The high molecular weight immunoreactive ACTH fraction (F-I), co-eluted with horse hemoglobin from a Sephadex G-75 column in 0.1M acetic acid, was essentially devoid of low molecular weight materials as revealed by polyacrylamide gel disc electrophoresis at pHs 9.5 and 4.3.<BR>Tryptic digestion of F-1 at pH 8.1 and 37°C for 4 hr with E/S of 1/100, followed by fractionation with a Sephadex G-75, resulted in the formation of lower molecular weight fragments. One fragment was eluted at the same position as that of porcine ACTH with a recovery of 86% of immunoactivity of F-I. Another fragment which was eluted last exhibited positive β-endorphin receptor binding activity.<BR>These results suggest the presence of a common precursor protein to ACTH and β-endorphin in human term placenta.
日本内分泌学会の論文