Isolation of camel brain actin--comparison of its biochemical properties with those of camel skeletal muscle, heart muscle and rabbit skeletal muscle actins.
1. Actins were purified from camel brain, skeletal muscle and heart muscle and their properties were compared. 2. Individual actins were homogeneous and comigrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). 3. Isoelectric focusing analysis of camel skeletal muscle and heart muscle actin showed a single polypeptide of the alpha-species, while camel brain actin showed two polypeptides of the beta- and gamma-species typical of non-muscle actin. 4. Actins from camel skeletal muscle and heart muscle showed a greater degree of similarity to each other and to rabbit skeletal muscle actin and showed some differences from camel brain actin, as confirmed by amino acid analysis and one-dimensional peptide mapping.
Duhaiman
A S
AS
Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
D000199:Actins / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002162:Camelus; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D009132:Muscles / Q000032:analysis; D009206:Myocardium / Q000032:analysis; D009928:Organ Specificity; D011817:Rabbits; D013045:Species Specificity
D000199:Actins; D000596:Amino Acids