Location of the disulfide bonds of the sweetness-suppressing polypeptide gurmarin.
The sweetness-suppressing polypeptide gurmarin has been isolated from the leaves of Gymnema sylvestre and consists of 35 amino acid residues including three intramolecular disulfide bonds. The primary structure has already been determined. The positions of the disulfide bonds were located, by a combination of mass spectrometric analysis and sequencing of cystine-containing peptides obtained by thermolysin-catalyzed hydrolysis of gurmarin, to be at Cys3-Cys18, Cys10-Cys23, and Cys17-Cys33.
Ota
M
M
Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki, Japan.
Ariyoshi
Y
Y
D000595:Amino Acid Sequence; D004220:Disulfides / Q000737:chemistry*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry; D018515:Plant Leaves / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry*; D010946:Plants, Medicinal / Q000737:chemistry
D004220:Disulfides; D010455:Peptides; D010940:Plant Proteins; C075206:Gurmarin protein, Gymnema sylvestre