Physical properties of myosin from aortic smooth muscle

Abstract

Porcine aortic myosin is a smooth muscle contractile protein similar to its striated muscle counterpart. Electrophoresis in sodium dodecyl sulfate indicates that the molecule consists of three classes of subunits with polypeptide chain molecular weights of 192,000, 19,000, and 15,000. At 277 nm the absorption spectrum gives an extinction coefficient for aortic myosin of 0.558 cm2/mg; the circular dichroism spectrum of the protein indicates that aortic myosin contains about 70% of its residues in the alpha-helical configuration. Amino acid analysis shows that the smooth muscle myosin has significantly more arginine and leucine and significantly less valine and isoleucine than rabbit skeletal muscle myosin. Other studies yielded these data: Vapp = 0.716 mL/g [eta] = 0.213 mL/mg, S20, w = 5.84 x 10(-13)S. Similar studies with rabbit skeletal muscle myosin indicate that Vapp = 0.711 mL/g and S20, w = 6.36 x 10(-13)S. These properties suggest that aortic myosin, like skeletal muscle myosin, behaves hydrodynamically like a rigid rod.