Position of the Disulfide Bond in Ovalbumins of Differing Heat Stability. Elimination of Thiol-Disulfide Interchange as a Mechanism for the Formation of the Ovalbumins

Abstract

Peptides containing the four cysteine and two half-cystine residues labelled with [2-14C]iodoacetic acid were isolated from thermolytic digests of reduced and S-carboxymethylated ovalbumin by paper ionophoresis, pH 6�4, descending paper chromatography and another ionophoresis at pH 1�9. These peptides were analysed for amino acids and the peptides identified with their position in the known linear sequence of the molecule.