Chromatographic and physical studies of tropomyosin in aqueous-organic media at low pH.
Non-cross-linked and disulfide-cross-linked two-chain molecules comprising the alpha and/or beta chains of rabbit skeletal tropomyosin were studied by electrophoretic, chromatographic and physical methods. Elution order on C4 reversed-phase high-performance liquid chromatography depends markedly on the number and position of the cross-links. In the C4 reversed-phase elution medium, cross-linked and non-cross-linked species are greater than 85% helical by circular dichroism, but the non-cross-linked elute later from high-performance size-exclusion chromatography (G4000) and have molecular mass of 31,000-41,000 dalton by equilibrium ultracentrifugation. The data suggest that in the C4 reversed-phase high-performance liquid chromatography elution medium non-cross-linked tropomyosin exists as amphipathic single-chain alpha-helices.
Crimmins
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Howard Hughes Medical Institute Core Protein/Peptide Facility, Washington University School of Medicine, St. Louis, MO 63110.
Holtzer
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D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000737:chemistry; D009206:Myocardium / Q000737:chemistry; D011489:Protein Denaturation; D011817:Rabbits; D014335:Tropomyosin / Q000737:chemistry / Q000302:isolation & purification*; D014461:Ultracentrifugation
D014335:Tropomyosin