title: Isolation of camel brain actin--comparison of its biochemical properties with those of camel skeletal muscle, heart muscle and rabbit skeletal muscle actins.
abstract: 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.
authors.affiliation: Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
authors.forename: A S
authors.initials: AS
authors.lastname: Duhaiman
mesh_terms: 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
chemical_list: D000199:Actins; D000596:Amino Acids