Nonmuscle caldesmon purified from cultured rat cells shows a molecular weight of 83,000 on SDS gels, Stokes radius of 60.5 A, and sedimentation coefficient (S20,w) of 3.5 in the presence of reducing agents. These values give a native molecular weight of 87,000 and a frictional ratio of 2.04, suggesting that the molecule is a monomeric, asymmetric protein. In the absence of reducing agents, the ...

Muscle cells infected at the permissive temperature with temperature-sensitive mutants of Rous sarcoma virus and shifted to the non-permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci. USA. 81:2265-2269). Work described in this paper demonstrates that the virally-infected cells are ...

Recessive mutant gene c in axolotl embryos results in an absence of normal heart function. Immunofluorescence studies were done to determine the distributions of myosin, tropomyosin and alpha-actinin in the hearts of normal and mutant siblings. Anti-myosin specifically stains the A bands of myofibrils in normal hearts and reveals a progressive increase in myofibril organization with development...

Tilapia is a very common aquaculture species in Taiwan and both the so-called freshwater tilapia (Oreochromis niloticus) and seawater tilapia (O. mossambica) are available. In order to characterize muscle tropomyosin from these tilapia and hybrid ones (O. mossambica × O. niloticus ), the biochemical properties of tropomyosin among these tilapia species were analysed. The nucleotide sequences of...

The length and amino acid sequence of the amino-terminal region of troponin T (TnT) is regulated by alternative mRNA processing in both mammals and birds. To study the function of this region, three forms of bovine cardiac TnT were compared: isoforms TnT1 and TnT2, which differ by the presence or absence of residues 15-19 and TnT 39-284. TnT 39-284 was prepared by chemical cleavage of TnT1 at C...

A theory developed previously for the stability of the native structure in two-chain, a-helical coiled coils is applied to singly (disulfide) cross-linked tropomyosin and to a singly (disulfide) cross-linked, synthetic, 43-residue peptide analogue (called here XY5) of tropomyosin. Algorithms are obtained from fits of extant data for the helix stability parameter (s) for each amino acid residue ...