Immunochemical studies on the light chains from skeletal muscle myosin

Autor: B.Z. Horváth, E. Gaetjens
Rok vydání: 1972
Předmět:
Zdroj: Biochimica et Biophysica Acta (BBA) - Protein Structure. 263:779-793
ISSN: 0005-2795
DOI: 10.1016/0005-2795(72)90062-1
Popis: 1. 1. The immunological properties of light chains from white muscle myosin have been examined by immunodiffusion and immunoelectrophoresis. Cross-reaction, showing immunological identity, occurred between two of the light chain fractions which are characterized by slow (L1) and fast (L3) electrophoretic mobility and molecular weights of 25 000 and 16 000, respectively. A third fraction (L2), with intermediate electrophoretic mobility and a molecular weight of 18 000, was found to be immunologically distinct from both L1 and L3. 2. 2. Radioimmunoassays showed that light chains bound to myosin did not react freely with their homologous antibodies but did so when the light chains were dissociated from myosin. The ATPase (EC 3.6.1.3) activity of myosin treated with light chain antisera was the same as that of native myosin. 3. 3. A sarcoplasmic fraction of muscle, which was free of myosin, reacted strongly with antisera to the light chains, indicating that at least two of the light chain fractions (L1 and L3) are present in the sarcoplasm of muscle independently of myosin. 4. 4. Myosin from chicken, frog, and rabbit muscle reacted with antisera to rabbit light chains, thus showing that in these three distinct classes of animals the light chains associated with myosin are antigenically related.
Databáze: OpenAIRE