A survey of interactions made by the giant protein titin.
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.
Soteriou
A
A
Department of Veterinary Medicine, Bristol University, Langford, UK.
Gamage
M
M
Trinick
J
J
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
D064211:Connectin; D009124:Muscle Proteins; D011494:Protein Kinases; D000659:AMP Deaminase; D009218:Myosins