An Immunochemical Approach to the Interaction of Light and Heavy Chains in Myosin

Abstract

Myosin from vertebrate skeletal muscles has two large polypeptide chains, each with a mass of about 200,000 daltons, and four smaller subunits in the range of 20,000 daltons (Lowey et al., 1969; Gershman et al., 1969; Gazith et al., 1970; Weeds and Lowey, 1971; Lowey and Risby, 1971). The heavy chains are folded into a rodlike α-helical conformation that extends over a length of about 1400 Å and terminates in two globular regions, each about 100 Å in diameter (Lowey et al., 1969). The light chains are located in the globular portion of the molecule where they are believed to be involved in determining the enzymic activity of myosin (Stracher, 1969; Driezen and Gershman, 1970).