Affiliation:
1. From the Department of Physiology, University of Maryland School of Medicine, Baltimore, Maryland, and the Marine Biological Laboratory, Woods Hole, Massachusetts
Abstract
Δ protein, a previously unreported fibrous protein with an electrophoretic mobility greater than that of myosin, is extracted from rabbit muscle by solutions of high ionic strength. This protein forms a complex with myosin, designated as Δ-myosin. Partial purification of Δ protein is achieved by two independent methods. In the first method alcohol fractionation is used. In the second, a solution of Salyrgan is used to dissociate the precipitated Δ-myosin complex. In each method further purification is obtained by preparative electrophoresis. Neither method yields a product which is entirely homogeneous. Tropomyosin is present as a contaminant in alcohol-fractionated preparations, and has been isolated and crystallized. All efforts to derive Δ protein from the previously known fibrous proteins of muscle have failed.
Publisher
American Physiological Society
Cited by
26 articles.
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