The components of troponin from chicken fast skeletal muscle. A comparison of troponin T and troponin I from breast and leg muscle.
The three components of troponin were prepared from chicken breast and leg muscle. The troponin I and T components were separated by chromatography on DEAE-cellulose after citraconylation and without the use of urea-containing buffers. The troponin I and C components were similar to their counterparts from rabbit fast skeletal muscle, and a comparison of the troponin I components from breast and leg  muscle by amino acid analysis, gel electrophoresis and peptide 'mapping' provides strong evidence for the identity of these proteins. The molecular weights of the troponin T components from breast and leg muscle were 33 500 and 30 500 respectively, determined by gel filtration. A comparison of these two proteins by methods similar to those used for the troponin I components suggested that they differed only in the N-terminal region of the sequence, the breast-muscle troponin T having an extra length of polypeptide chain of approx. 24 residues that is rich in histidine and alanine. The N-terminal hexapeptide sequence, however, is the same in both proteins and is (Ser,Asx,Glx)Thr-Glu-Glu. The genetic implications of these findings are considered.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D009132:Muscles / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D013057:Spectrum Analysis; D014336:Troponin / Q000032:analysis*
D000596:Amino Acids; D009124:Muscle Proteins; D010446:Peptide Fragments; D014336:Troponin