Premium
Studies on the Subunits Involved in the Interaction of Soybean 11S Protein and Myosin
Author(s) -
PENG I. C.,
DAYTON W. R.,
QUASS D. W.,
ALLEN C. E.
Publication year - 1982
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.1365-2621.1982.tb12927.x
Subject(s) - myosin , chemistry , size exclusion chromatography , protein subunit , gel electrophoresis , electrophoresis , biochemistry , polyacrylamide gel electrophoresis , protein–protein interaction , soy protein , chromatography , biophysics , biology , enzyme , gene
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.