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METACHROMATIC EFFECT IN HOMOLOGOUS GROUPS OF WHEAT, BARLEY AND RYE PROLAMINS
Author(s) -
CHIRDO FERNANDO GABRIEL,
FOSSATI CARLOS ALBERTO,
AÑON MARÍA CRISTINA
Publication year - 1994
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1994.tb00496.x
Subject(s) - metachromasia , polyacrylamide gel electrophoresis , glutenin , chemistry , sodium dodecyl sulfate , biochemistry , gel electrophoresis , coomassie brilliant blue , prolamin , storage protein , staining , chromatography , biology , enzyme , genetics , gene , protein subunit
The metachromatic behavior of wheat, barley and rye prolamins, separated by polyacrylamide gel electrophoresis (PAGE) and staining with Coomassie Brilliant Blue R‐250, is described. Metachromasia was detected both visually and by double beam densitometric analysis of sodium dodecyl sulfate‐PAGE and acidic‐PAGE (A‐PAGE) at pH 3.1. Differential readings were recorded at 525 nm, with reference at 625 nm. Metachromatic components were found in the homologous groups, (a) S‐poor prolamins: ω‐gliadins, C‐hordeins, ω‐secalins and (b) high molecular weight (HMW)‐prolamins: HMW‐glutenins, D‐hordeins and HMW‐secalins, in wheat, barley and rye, respectively. In contrast, proteins having this characteistic have not been found in oat.