Relations of the spectrin complex of human erythrocyte membranes to the actomyosins of muscle cell

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Abstract
Important similarities are reported between human smooth muscle actomyosin and the human erythrocyte spectrin complex, primarily components 1, 2, and 5. The actin-like protein, component 5, is identical with human uterine actin in its ability to form 50-70 .ANG. filaments, to stimulate myosin ATPase activity, and to bind rabbit heavy meromyosin specifically. Antibodies to human smooth muscle myosin (uterine) were prepared which were monospecific. A weak but specific cross-reaction of these antisera with components 1 and/or 2 (spectrin) was characterized and at least 25% of the antimyosin antibodies showed a low affinity reaction with spectrin. Antibodies generated against a soluble complex of spectrin components 1 and 2 reacted only with component 1 and did not cross-react with myosin. In addition to these structural similarities between smooth muscle actomyosin and the spectrin complex, spectrin is involved in ATP-dependent erythrocyte shape changes and, therefore, the spectrin complex is also a mechanochemical protein system.
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