Amino acid sequence of a soybean (Glycine max) seed polypeptide having a poly(L-aspartic acid) structure.
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.
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides; D014674:Plant Proteins, Dietary / Q000302:isolation & purification; D030262:Soybean Proteins; D014357:Trypsin
D010446:Peptide Fragments; D010455:Peptides; D014674:Plant Proteins, Dietary; D030262:Soybean Proteins; C017645:polyaspartate; D014357:Trypsin