[Studies on immunoreactive ACTH from human term placenta. (I) Detection of a high molecular weight-immunoreactive ACTH in term placenta (author's transl)].
Nihon Naibunpi Gakkai Zasshi
; 57(6): 880-90, 1981 Jun 20.
Article
en Ja
| MEDLINE
| ID: mdl-6269917
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--39 alpha) 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. 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. Tryptic digestion of F-1 at pH 8.1 and 37 degrees 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 immunoreactivity of F-I. Another fragment which was eluted last exhibited positive beta-endorphin receptor binding activity. These results suggest the presence of a common precursor protein to ACTH and beta-endorphin in human term placenta.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Placenta
/
Hormona Adrenocorticotrópica
Tipo de estudio:
Diagnostic_studies
Límite:
Female
/
Humans
/
Pregnancy
Idioma:
Ja
Revista:
Nihon Naibunpi Gakkai Zasshi
Año:
1981
Tipo del documento:
Article
Pais de publicación:
Japón