Abstract
Abstract
Atrial natriuretic factor (ANF), released by the isolated perfused rat heart, was extracted from the perfusates by C18 Sep-Pak cartridges and then isolated by immunoaffinity chromatography and by reverse phase HPLC. About 500 ng of immuno-reactive material were so obtained and submitted to amino acid sequencing. The C-terminal Tyr was detected by radiolabel1ing. Identification of these residues indicated that the primary structure corresponds to ANF (Ser 99 - Tyr 126) which is identical to the circulating form in the rat. These results indicate that the ANF released by the atria corresponds to a short peptide. Therefore, its maturation process may therefore take place either intracellular^ or during secretion and implicates a tryptic-like cleavage after a single Arg residue in position 98.
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