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Protein‐Protein Interactions Between Soybean Beta‐conglycinin (B 1 ‐B 6 ) and Myosin
Author(s) -
PENG I. C.,
NIELSEN S.S.
Publication year - 1986
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1986.tb13886.x
Subject(s) - myosin , turbidity , solubility , chemistry , electrophoresis , polyacrylamide gel electrophoresis , acrylamide , beta (programming language) , gel electrophoresis , chromatography , biochemistry , biology , enzyme , polymer , organic chemistry , ecology , computer science , programming language , copolymer
Protein‐protein interactions between soybean beta‐conglycinin (B 1 ‐ B 6 ) and myosin were studied by turbidity, solubility and SDS‐poly‐ acrylamide gel electrophoresis (SDS‐PAGE) analysis. Turbidity and solubility studies showed that, under the experimental conditions used, these proteins interacted at temperatures between 60° and 100°C, while SDS‐PAGE analysis indicated that the interaction also occurred at 50°C. The interasction was such that no detectable complexing between these two proteins was observed. The presence of beta‐conglycinin resulted in diminished aggregations of myosin heavy chains between 50° and 100°C.