Effect of trichloroacetic acid on the isolation of tropomyosin from sea urchin lantern muscle.
Sea urchin lantern muscle tropomyosin showed two components in sodium dodecyl sulfate (SDS) gel electrophoresis in the presence of 5 M urea, although the molecular weights of these components were apparently identical. One of these components seemed to have been digested with an enzyme such as carboxypeptidase, and the tropomyosin had lost the abilities to polymerize and to bind to actin. A crude extract prepared from the lantern muscle treated with trichloroacetic acid (TCA) contained predominantly tropomyosin. Tropomyosin purified from TCA-treated lantern muscle seemed to be intact and retained the ability to bind to actin.
D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D009132:Muscles / Q000032:analysis*; D011817:Rabbits; D012617:Sea Urchins; D014238:Trichloroacetic Acid / Q000494:pharmacology*; D014335:Tropomyosin / Q000302:isolation & purification*
D014335:Tropomyosin; D014238:Trichloroacetic Acid; D002268:Carboxypeptidases; D043422:Carboxypeptidases A