The atrial natriuretic factor (ANF) secreted from rat cardiocytes in culture was purified and characterized. The purification procedure involves extraction of ANF by activated Vycor glass, followed by HPLC on C18 μ Bondapak and Vydac columns. The detection of ANF in column eluates was performed by a simple and sensitive radioimmunoassay. The amino acid composition and N-terminal amino acid sequencing appeared to be identical to the Arg 101 - Tyr 126 peptide. The isolated ANF showed biological activity, inhibiting basal and ACTH-stimulating aldosterone secretion from rat zona glomerulosa cells with the same potency as the synthetic peptide.
|Number of pages||9|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - Aug 15 1985|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology