The sequence of an atriopeptigen: A precursor of the bioactive atrial peptides |
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Authors: | D.M. Gelher M.G. Currie N.R. Siegel K.F. Fok S.P. Adams P. Needleman |
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Affiliation: | 1. Department of Pharmacology, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, Mo. 63110 USA |
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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. |
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Keywords: | To whom request for reprints should be addressed. |
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