Amino acid sequence of a soybean (Glycine max) seed polypeptide having a poly(L-aspartic acid) structure

J Biol Chem. 1987 Aug 5;262(22):10502-5.


A polypeptide of Mr 4400 was isolated from soybean (Glycine max) seeds by extraction with 60% ethanol followed by ion-exchange and reverse-phase chromatography. The peptide contains an unusually high amount of aspartic acid residues (approximately 25%, and hence is designated as soybean aspartic acid-rich peptide). Its complete primary structure was determined by conventional methods to be the following. Ser-Lys-Trp-Gln-His-Gln-Gln-Asp-Ser-Cys-Arg-Lys-Gln-Leu-Gln-Gly-Val-Asn- Leu-Thr-Pro-Cys-Glu-Lys-His-Ile-Met-Glu-Lys-Ile-Gln-Gly-Arg-Gly-Asp-Asp- Asp-Asp-Asp-Asp-Asp-Asp-Asp A striking features of this primary structure is the presence of a poly(L-aspartic acid) sequence at the carboxyl terminus, and this polyaspartyl segment was found to precipitate bovine trypsin. The presence of the putative cell attachment sequence Arg-Gly-Asp was also noted.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Peptide Fragments / isolation & purification
  • Peptides*
  • Plant Proteins, Dietary* / isolation & purification
  • Soybean Proteins
  • Trypsin


  • Peptide Fragments
  • Peptides
  • Plant Proteins, Dietary
  • Soybean Proteins
  • polyaspartate
  • Trypsin