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.