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Reaction of wheat proteins with sulphite. III. Measurement of labile and reactive disulphide bonds in gliadin and in the protein of aleurone cells
Author(s) -
Stevens Derrick J.
Publication year - 1973
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740240304
Subject(s) - aleurone , chemistry , gliadin , endosperm , urea , biochemistry , organic chemistry , chromatography , gluten
Qualitative evidence for the intra‐chain character of the disulphide bonds in gliadin, has been confirmed by quantitative measurement of the total number of bonds, and of the number reacting with sulphite under differing conditions of urea concentration. The results indicated that gliadin was composed of single polypeptide chains, which contained an average of four disulphide bonds each, in labile H‐bonded configurations. Similar measurements on the protein of wheat aleurone cells, showed the presence of a high proportion of thiol groups, and a relatively low content of disulphide groups. All of the groups were accessible to reaction with sulphite, which implied that short polypeptide chains were involved in this soluble protein system. The results are discussed in relation to the development of protein in the endosperm, and in the aleurone layer, and to the rǒle of both types of protein in germination.