Cloning, sequencing and expression of a full-length rabbit fast skeletal troponin-C cDNA.
A full-length cDNA coding for troponin-C isolated from an adult rabbit fast skeletal muscle library has been sequenced and expressed in an E. coli host. The amino acid sequence derived from the coding region agrees with the published protein sequence except that the first two residues are reversed. The expressed protein was found to be identical to purified rabbit skeletal troponin-C based on electrophoretic mobilities in polyacrylamide gels containing either SDS or urea, and on immunoblotting. These results establish that our troponin-C cDNA clone is suitable for site-directed mutagenesis studies on the structure and function of troponin-C.
Chen
Q
Q
Department of Muscle Research, Boston Biomedical Research Institute, MA 02114.
Taljanidisz
J
J
Sarkar
S
S
Tao
T
T
Gergely
J
J
D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D005786:Gene Expression Regulation; D005822:Genetic Vectors; D008969:Molecular Sequence Data; D011817:Rabbits; D014336:Troponin / Q000235:genetics* / Q000302:isolation & purification / Q000502:physiology; D019209:Troponin C
D014336:Troponin; D019209:Troponin C; D004247:DNA