Assignments of the disulphide bonds in the sweet-tasting protein thaumatin I

The disulphide linkages of the 16 half-cyteine residues in the sweet-tasting protein thaumatin have been investigated by enzymatic hydrolysis of the intact molecule. The peptides obtained after proteolytic cleavage with trypsin and pepsin, and in one case with chymotrypsin have been purified by gel...

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Veröffentlicht in:	European journal of biochemistry 1984-01, Vol.144 (1), p.41-45
Hauptverfasser:	Van Der Wel, H, Iyengar, R B, Van Brouwershaven, J, Van Wassenaar, PD, Bel, W J, Van Der Ouderaa, FJG
Format:	Artikel
Sprache:	eng
Schlagworte:	cysteine disulfide bonds electrophoresis pepsin peptide mapping sweetness thaumatin trypsin
Online-Zugang:	Volltext
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