The subunits and biological activity of polymorphic forms of tropomyosin

Abstract

1. Free thiol groups were shown to be essential for tropomyosin to effect maximum inhibition of the Ca2+-stimulated ATPase (adenosine triphosphatase) of desensitized actomyosin but not for its activity in the regulatory-protein system. 2. The activity of tropomyosin on the Mg2+-stimulated ATPase in the regulatory-protein system was more susceptible to enzymic digestion and thermal denaturation than its effect on the Ca2+-stimulated ATPase of actomyosin. 3. Rabbit skeletal tropomyosin migrated as two distinct electrophoretic components in the presence of sodium dodecyl sulphate and urea and as four components on isoelectric focusing in urea. 4. The two main subunits present in rabbit skeletal tropomyosin, which have been named the α- and β-chains, were separated by chromatography on CM-cellulose in urea at pH4.0. They were shown to be virtually identical in amino acid composition, except for their cysteine contents. The α2 and β2 forms of tropomyosin possessed all the biological activities characteristic of normal tropomyosin preparations. 5. In skeletal muscle the α and β components of tropomyosin were present in the proportion of 4:1. Somewhat lower ratios were obtained in skeletal muscle of sheep, pig and cow. 6. Tropomyosin isolated from cardiac muscle and Pecten maximus adductor muscle migrated as one band only. These tropomyosins possessed similar biological activities to those isolated from skeletal muscle.