DISC ELECTROPHORESIS OF MYOSIN AND MYOSIN DERIVATIVES IN DILUTE POLYACRYLAMIDE GELS

Although its large size and insolubility in dilute salt solutions have previously prevented analysis of myosin by disc electrophoresis, useful migration of this protein was obtained upon electrophoresis in dilute polyacrylamide gels containing 9 M urea. Under these conditions, substantial heterogeneity of the largest subunits was detected. Electrophoretic analyses of acetylated and succinylated myosin preparations in 2.6% (w/v) acrylamide in the presence or absence of urea also have numerous bands in addition to those previously attributed to small subunits of myosin. Although the significance of the multiple bands must still be viewed with some reservations, it is clear that electrophoresis in dilute polyacrylamide gels can achieve separations of very large polypeptide chains which appear homogeneous by other methods of analysis. © 1969.