The sequence of an atriopeptigen: a precursor of the bioactive atrial peptides

Biochem Biophys Res Commun. 1984 Jun 29;121(3):802-7. doi: 10.1016/0006-291x(84)90749-6.

Abstract

The high molecular weight fraction ( atriopeptigen -APG) obtained by gel filtration chromatography of rat atrial extracts was fractionated by isoelectric focusing and reverse phase HPLC to obtain a pure APG. Purification of cyanogen bromide digests of the crude high molecular weight fraction resulted in the isolation of a single biologically active cyanogen bromide cleavage peptide. Sequence analyses of these peptides coupled with recent reports of sequence analyses of intermediate molecular weight atrial peptides ( Thibault , et al. (1984) FEBS Letters 167, 352-356, and Kangwa , et al., Biochem. Biophys. Res. Commun 119, 933-940) provide the complete primary structure of an 111 residue APG.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Atrial Natriuretic Factor
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Cyanogen Bromide
  • Heart Atria / analysis
  • Molecular Weight
  • Muscle Proteins / isolation & purification*
  • Peptide Fragments / isolation & purification
  • Protein Precursors / isolation & purification*
  • Rats

Substances

  • Muscle Proteins
  • Peptide Fragments
  • Protein Precursors
  • Atrial Natriuretic Factor
  • Cyanogen Bromide