Studies on the Subunits Involved in the Interaction of Soybean 11S Protein and Myosin |
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| Authors: | I C PENG W R DAYTON D W QUASS C E ALLEN |
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| Affiliation: | Authors Dayton and Allen are with the Dept. of Animal Science, Univ. of Minnesota, St. Paul, MN 55108.;Author Peng, formerly with the Univ. of Minnesota, is now affiliated with the Dept. of Animal Sciences, Purdue Univ., West Lafayette, IN 47907. Author Quass is with Land O'Lakes, Minneapolis, MN 55440. Address inquiries to Dr. Allen. |
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| Abstract: | 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. |
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