The Inoorporation of [35s]Oysteine into the Proteins of Dough by Disulphide-Sulphydryl Interohange

Abstract

[35S]Cysteine was added, during mixing, to doughs made from wheat flour, in amounts which did not significantly affect the level of endogenous diffusible sulphydryl compounds in flour and which produced no change in the rheological properties of the dough. The doughs were fractionated by ultracentrifugation and analysis of the distribution of the isotope in the dough fractions demonstrated that [S6S]cysteine was bound to both soluble and gluten proteins by disulphide bonds. [14C]Leucine did not become bound to the fractions of dough under the same conditions.