Proteins of the contractile mechanism of mammalian smooth muscle and their possible location in the cell

Abstract

Dorothy M. Needham speaking. Since the pioneer work of Csapo and his colleagues, beginning about fifteen years ago, it has been realized that from uterine smooth muscle can be extracted a protein closely resembling skeletal-muscle actomyosin in its viscous behaviour, sedimentation rate and electrophoretic mobility. (See, for example, Csapo 1948, 1949, 1950, 1959; Csapo, Erdos, Naeslund & Snellman 1950; Naeslund & Snellman 1951). Later work, in which the properties of purified preparations of myosin, actin and actomyosin have been studied, bears out these earlier conclusions. Thus, for example, we have shown (Needham & Williams 1963 b ) that skeletal-muscle myosin will react normally with uterus actin to give the highly viscous actomyosin; and similarly uterus myosin with skeletal-muscle actin. In both types of experiment the results indicated that the two proteins associated together in about the same proportions as when both are derived from skeletal muscle. Uterus actomyosin may be fragmented by carefully controlled trypsin treatment giving light and heavy meromyosins which, so far as they have been studied, show similar properties to the meromyosins from skeletal-muscle actomyosin (Needham & Williams 1959; Cohen, Lowey & Kucera 1961). Smooth muscle, however, does contain very strikingly less actomyosin than striated muscle, only 6 to 10 mg/g wet wt as compared with about 70 mg/g wet wt in skeletal muscle (Needham & Williams 1963 a ).