Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Location of the Disulfide Bonds of the Sweetness-suppressing Polypeptide Gurmarin
Masafumi OtaYasuo Ariyoshi
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JOURNAL FREE ACCESS

1995 Volume 59 Issue 10 Pages 1956-1957

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Abstract

The sweetness-suppressing polypeptide gurmarin has been isolated from the leaves of Gyntnenla 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 CysFCys18, Cys10-Cys23, and Cys17-Cys33.

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