Purification of rabbit skeletal muscle troponin C.
Troponin C binds to phenyl-Sepharose in the presence of Ca2+ and can be eluted with EDTA. This property was used as an essential step in the purification of this protein from rabbit skeletal muscle. Troponin C was extracted with 6M urea from extensively washed ground muscle. The protein was bound to and eluted from DEAE-Sephadex, fractionated by size on Sephadex G75, and in a final step purified from UV-absorbing non-protein impurities on phenyl-Sepharose. The total yield of electrophoretically pure protein was 60 mg per 100 g of muscle, which is considerably higher than that previously obtained.
Thulin
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Department of Physical Chemistry 2, University of Lund, Sweden.
Vogel
H J
HJ
D000818:Animals; D002850:Chromatography, Gel / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism*; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet; D014336:Troponin / Q000302:isolation & purification*; D019209:Troponin C
D014336:Troponin; D019209:Troponin C