title: Analytical sedimentation studies of turkey gizzard myosin light chain kinase and telokin.
abstract: Sedimentation equilibrium and velocity studies were performed with turkey gizzard myosin light chain kinase (MLCK) and telokin, a small protein apparently corresponding to the sequence of the COOH-terminal end of MLCK. The measurements carried out with MLCK give values for the monomer molecular weight (M(r)), sedimentation coefficient (S20 degrees,w), and virial coefficient (A2) of 108,000, 3.74 S, and -1.95 x 10(-4) mol.ml.g-2, respectively. In the case of telokin, M(r) = 18,500; S20 degrees, w = 1.63 S; and A2 = 5.81 x 10(-4)mol.ml.g-2. Combination of the results of the two kinds of experiment shows that MLCK is a rod-shaped molecule (a/b = 18.9) with a Stoke's radius of 69 A. Telokin is also elongated (a/b = 8.3) with a Stoke's radius of 29 A. MLCK apparently exhibits self-association, with 15% of the protein sedimenting as a dimer in the experiments.
authors.affiliation: Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
authors.forename: J
authors.initials: J
authors.lastname: Ausio
authors.forename: D A
authors.initials: DA
authors.lastname: Malencik
authors.forename: S R
authors.initials: SR
authors.lastname: Anderson
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005895:Gizzard, Avian / Q000201:enzymology; D008433:Mathematics; D008962:Models, Theoretical; D008970:Molecular Weight; D009124:Muscle Proteins / Q000737:chemistry* / Q000302:isolation & purification; D009130:Muscle, Smooth / Q000201:enzymology; D009219:Myosin-Light-Chain Kinase / Q000737:chemistry* / Q000302:isolation & purification; D010446:Peptide Fragments; D010455:Peptides; D014422:Turkeys; D014461:Ultracentrifugation
chemical_list: D000596:Amino Acids; D009124:Muscle Proteins; D010446:Peptide Fragments; D010455:Peptides; C060640:telokin; D009219:Myosin-Light-Chain Kinase