The amino acid sequence in a hypertensin

Abstract

A hypertensin peptide isolated from ox serum was subjected to end group analysis by the fluoro-2:4-dinitrobenzene method, enzymic hydrolysis with carboxypeptidase, trypsin, chymotrypsin and aminopeptidase, partial acid hydrolysis and the Edman stepwise-degradation method. The products of reaction were studied by paper chromatography and paper electrophoresis. The amino acid sequence was shown to be aspartic acid, arginine, valine, tyrosine, valine, histidine, proline, phenylalanine, histidine, leucine. On the basis of digestion by amino peptidase it is believed that all the amino acids have the L-configuration and that the N-terminal residue is aspartic acid, not asparagine.