C-protein from chicken pectoralis muscle has been purified by sequential DEAE-Sephadex and hydroxyapatite chromatography and examined by transmission electron microscopy after spraying in glycerol onto mica and replicating by rotary shadowing with platinum. The most frequently observed particles were of three forms: rod-shaped, U-shaped and V-shaped. Within a size range of 15–40 nm these three groups accounted for 70% of over 800 particles categorized and measured. The remaining particles could not be classified. Since the relative abundance of each of these three forms was well in excess of any of the contaminating proteins detectable by SDS-polyacrylamide gel electrophoresis, we conclude that these variant forms represent C-protein molecules in differing conformations and/or deformations. Particles were observed which were intermediate between rod-shaped and tightly curved U-shaped forms, and between rod and acutely angled V-shaped forms. These results are compatible with a molecular model of a 32 nm × 3 nm flexible, rod-shaped C-protein monomer similar to one previously proposed from hydrodynamic studies and extend recent observations on the ultrastructure of cardiac C-protein.
Infrequently, a discontinuously larger V-shaped form was seen, possibly representing a C-protein dimer.
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Swan, R.C., Fischman, D.A. Electron microscopy of C-protein molecules from chicken skeletal muscle. J Muscle Res Cell Motil 7, 160–166 (1986). https://doi.org/10.1007/BF01753417
- Transmission Electron Microscopy
- Skeletal Muscle
- Relative Abundance