[Isolation of myosin light chain from porcine heart by preparative electrophoresis and study of the polypeptides obtained by cyanogen bromide action].
A simple, rapid and efficient procedure is developed to isolate proteins with identical or different isoelectric points such as pig cardiac myosin light chains. Preparative electrophoresis on discontinuous polyacrylamide slab gels in the presence of urea allows a very good separation of each light chain (L27 and L18) and heavy chain from highly purified myosin. An original elution procedure of the proteins fixed and localized by amido schwartz allows the isolation of the L27 and L18 light chains in quantities sufficient to carry out structural studies. Homogeneity of light chains thus isolated is checked by the analysis of cyanogen bromide peptides. Structural similarities can be demonstrated between myosin light chains of beef and pig heart.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D009206:Myocardium / Q000032:analysis*; D009218:Myosins / Q000302:isolation & purification; D010446:Peptide Fragments / Q000032:analysis; D010455:Peptides / Q000032:analysis; D013045:Species Specificity; D013552:Swine
D000596:Amino Acids; D046911:Macromolecular Substances; D010446:Peptide Fragments; D010455:Peptides; D009218:Myosins; D003488:Cyanogen Bromide
Isolement des chaînes légères de la myosine cardiaque de porc par électrophorèse préparative et étude des polypeptides obtenus après action du bromure de cyanogène.