Structural studies on the light chains of myosin

Rabbit skeletal muscle myosin contains two large polypeptide chains of molecular weight about 200,000daltons (the heavy chains) (Gershman et al., 1969; Gazith et al., 1970) and several small poly-peptide chains of about 20,000 daltons (the light chains). These light chains are nonconvalentty bound to the heavy chains and can be dissociated under a variety of conditions, all of which result in loss of ATPase activity: with alkali (Kominz et al., 1959), urea (Tsao, 1953), guanidinc hydrochloride (Dreizen et al., 1967), or by acylation of the e-amino groups of lysine with acetic anhydride (Locker and Hagyard, 1967a). They appear to be required for the enzymic activity of myosin, since they can be removed under much milder condition