Human skeletal muscle proteins. The primary structure of troponin C.
The primary structure of the major component of human skeletal muscle troponin C has been established. The troponin C was purified by ammonium sulphate and isoelectric fractionation, followed by two chromatographic steps on DEAE Sephadex. The sequence was determined from the different overlapping enzymic peptides and by dansyl-Edman degradation. The only difference between rabbit skeletal muscle troponin C and the major component of human skeletal troponin C was found at position 112: Ala (rabbit), Pro (human). The partial amino acid sequence of the first 86 residues of the minor component of human skeletal troponin C was found to resemble the troponin C from bovine cardiac muscle. The only difference between them, has tentatively been located at position 62: Glu (human), Asp (bovine). These similarities suggest that troponin C is, from the point of view of molecular, one of the most conservative proteins so far studied.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D005075:Biological Evolution; D006801:Humans; D009124:Muscle Proteins / Q000302:isolation & purification; D009132:Muscles; D010446:Peptide Fragments / Q000032:analysis; D013381:Subtilisins; D013820:Thermolysin; D014336:Troponin / Q000302:isolation & purification; D014357:Trypsin
D000596:Amino Acids; D009124:Muscle Proteins; D010446:Peptide Fragments; D014336:Troponin; D013381:Subtilisins; D014357:Trypsin; D013820:Thermolysin