Isolation of Myosin and Actin from Chicken Muscle

 

Richard H. Racusen and Katerina V. Thompson

Tested Studies in Laboratory Teaching, 1997, Volume 18

Abstract

Using modifications of classic biochemical procedures for purifying the muscle contractile proteins, myosin and actin, we devised a 3-hour laboratory on the biochemistry of muscle that is appropriate for students in an introductory college biology course. The protocol begins with the extraction of small pieces of frozen chicken muscle in high salt (enhances myosin recovery) and low salt (enhances actin recovery) buffers. Solubilized myosin is induced to form visible filaments by lowering the ionic strength of the buffer, and a small pellet of enriched myosin is collected by centrifugation. Aliquots of both myosin and actin preparations are prepared for electrophoresis on small SDS, polyacrylamide slab gels. Completed electropherograms are stained, and students determine the molecular weights of gel bands. These data are then compared to known structural models of myosin and actin subunits and fragments.

Keywords:  muscle, protein electrophoresis, actin, myosin

Boston University (1996)