Protein‐protein interaction between soybean 11S protein and myosin in a buffer system was studied using gel filtration chromatography and electrophoresis after incubating the single or combined proteins at temperatures between 4°C and 100°C. The elution profiles of 11S protein and myosin indicated that interaction between these two proteins occurred only at temperatures between 85° C and 100°C. The degree of interaction increased as temperature increased from 85 to 100°C. The interaction was not between native soy 11S and myosin, but between partially dissociated soy 11S (intermediary subunits, IS) or fully dissociated soy 11S (basic subunits) and myosin heavy chains. The rate of interaction was proposed as being more rapid between myosin and the basic subunits than between myosin and IS.
|Original language||English (US)|
|Number of pages||7|
|Journal||Journal of food science|
|State||Published - Nov 1982|