title: Purification and complete amino acid sequence of beta-rat atrial natriuretic polypeptide (beta-rANP) of 5,000 daltons.
abstract: A survey for natriuretic factors in rat atrial extract was performed by the aid of a simple assay for the relaxant effect on the contractility of chick rectum, in a manner similar to our previous purification of alpha-human atrial natriuretic polypeptide (alpha-hANP). Three distinct components (alpha, beta and gamma) of a potent relaxant activity with varying molecular weights, were found in the chromatographic regions of a crude extract. From the beta-component of rectum activity corresponding to about 5,000 daltons, a 48-amino acid peptide has been purified to homogeneity and found to elicit a potent natriuretic activity, when injected into the assay rats. Accordingly, the peptide was designated as "beta-rat atrial natriuretic polypeptide (beta-rANP)". The complete amino acid sequence of the peptide has been determined by microsequencing the S-carboxymethylated beta-rANP and its tryptic peptides.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016275:Atrial Function; D009320:Atrial Natriuretic Factor; D002645:Chickens; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006321:Heart / Q000502:physiology*; D009124:Muscle Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D009126:Muscle Relaxation / Q000187:drug effects; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D012007:Rectum / Q000187:drug effects
chemical_list: D009124:Muscle Proteins; D010446:Peptide Fragments; D009320:Atrial Natriuretic Factor