Isolation and characterization of hog thyroid actin.
When the thyroglobulin content is subtracted, actin represents approximately 4.6% of the total protein content in the hog thyroid gland. Actin has been isolated from acetone-dehydrated slices and purified to homogeneity by gel filtration, DEAE-cellulose chromatography and two polymerization-depolymerization cycles. Purified actin (Mr = 42000) contains the beta and gamma species with a 2 to 1 stoichiometry. In the presence of 0.1 M KCl and 2 mM MgCl2 thyroid actin polymerized into 6 nm diameter filaments; under these conditions the critical concentration was 30 micrograms/ml and the intrinsic viscosity 4.7 dl/g.
D000096:Acetone; D000199:Actins / Q000302:isolation & purification* / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001704:Biopolymers; D008722:Methods; D013552:Swine / Q000378:metabolism; D013961:Thyroid Gland / Q000032:analysis*
D000199:Actins; D000596:Amino Acids; D001704:Biopolymers; D000096:Acetone