Affinity-chromatographic isolation and some properties of troponin C from different muscle types.
1. The formation of a complex between troponin I and troponin C that is stable in 6M-urea and dependent on Ca2+ was demonstrated in extracts of vertebrate striated and smooth muscles. 2. A method using troponin I coupled to Sepharose is described for the rapid isolation of troponin C from striated and smooth muscles of vertebrates. 3. Troponin C of rabbit cardiac muscle differs significantly in amino acid composition from troponin C of skeletal muscle. The primary structures of troponin C of red and white skeletal muscle are very similar. 4. The troponin C-like protein isolated from rabbit uterus muscle has a slightly different amino acid composition, but possess many similar properties to the forms of troponin C isolated from other muscle types. 5. The electrophoretic mobilities of the I-troponin C complexes formed from components isolated from different muscle types are determined by the troponin I component.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D009124:Muscle Proteins / Q000302:isolation & purification*; D009130:Muscle, Smooth / Q000032:analysis; D009132:Muscles / Q000032:analysis; D011817:Rabbits; D014336:Troponin / Q000031:analogs & derivatives / Q000302:isolation & purification*
D000596:Amino Acids; D009124:Muscle Proteins; D014336:Troponin