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Purothionin analogues from barley flour
Author(s) -
Redman D. G.,
Fisher N.
Publication year - 1969
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.2740200715
Subject(s) - composition (language) , barley flour , amino acid , globulin , chemistry , food science , peptide , electrophoresis , biochemistry , wheat flour , biology , chromatography , philosophy , linguistics , immunology
Acid treatment of a light‐petroleum extract of barley flour yielded two proteins (termed hordothionins) closely similar in electrophoretic behaviour to the purqthionin doublet obtained from wheat by the same procedure. The major (faster) component, hordothionin a has been obtained apparently pure. Comparison of its amino acid composition, peptide maps, immunological reactions and C‐terminal end group with those of purothionin a has confirmed the relationship between the proteins from the two genera although some differences in amino acid composition and sequence have been found. Extraction of barley flour with buffered saline followed by acid treatment yielded proteins with similar properties to the hordothionins; this supports previous observations on the relationship between the purothionins and their corresponding globulins.