Record Details

Title:
Heat-induced interactions between soybean proteins: preferential association of 11S basic subunits and beta subunits of 7S
Publication date:
1984
Summary:
Heat-induced interactions between soy 7S and 11S globulins were studied. Heating caused dissociation of both 7S and 11S globulins; the dissociated subunits of 7S and 11S globulins subsequently interacted with each other, forming soluble macrocomplexes having molecular weights over one million. Two-dimensional gel electrophoretic analysis revealed that the macrocomplexes contained predominantly the basic subunits of 11S globulin and the beta subunit of 7S globulin; little of the alpha and alpha` subunits of 7S globulin was present in these complexes, indicating that the basic subunits of 11S have higher affinity for the beta subunit. The results also indicated that the interaction between the basic subunits and the beta subunit is predominantly electrostatic in nature. Furthermore, disulfide bonds between the basic subunits are also involved in the formation of soluble macrocomplexes. [AS/SS]
Call number:
A:PS
Journal citation:
Contact information:
harvest@worldveg.org

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 Record created 1985-05-31, last modified 2019-03-04


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