title: A survey of interactions made by the giant protein titin.
abstract: A simple solid-phase binding assay was used to screen for interactions that the giant myofibrillar protein titin makes with other sarcomeric proteins. The titin used in the tests was purified by a modified procedure that results in isolation of approximately 20 mg relatively undegraded protein in < 24 h. In addition to the approximately 3 MDa polypeptide, bands at approximately 160 kDa and approximately 100 kDa were also consistently seen on gels. Binding of titin to myosin, C-protein, X-protein and AMP-deaminase was observed. The interaction with myosin appears to be with the light meromyosin part of the molecule.
authors.affiliation: Department of Veterinary Medicine, Bristol University, Langford, UK.
authors.forename: A
authors.initials: A
authors.lastname: Soteriou
authors.forename: M
authors.initials: M
authors.lastname: Gamage
authors.forename: J
authors.initials: J
authors.lastname: Trinick
mesh_terms: D000659:AMP Deaminase / Q000378:metabolism; D000818:Animals; D064211:Connectin; D009124:Muscle Proteins / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism; D011485:Protein Binding; D011494:Protein Kinases; D011817:Rabbits; D012518:Sarcomeres / Q000378:metabolism
chemical_list: D064211:Connectin; D009124:Muscle Proteins; D011494:Protein Kinases; D000659:AMP Deaminase; D009218:Myosins