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J. Biochem, 1976, Vol. 80, No. 1 89-99
© 1976 Japanese Biochemical Society

research-article

Interaction of Tropomyosin with Troponin Components

Renata DABROWSKA*, Zoya PODLUBNAYA**, Ewa NOWAK* and Witold DRABIKOWSKI*

*Department of Biochemistry of Nervous System and Muscle, Nencki Institute of Experimental Biology Warsaw, Poland
**Institute of Biophysics Pushchino on Oka, U.S.S.R

1. The TN-T and TN-I components of troponin both interact with tropomyosin and cause its precipitation in 0.1 M KCl at neutral pH. The precipitate contains both end-to-end and side-by-side aggregates of tropomyosin molecules.

2. The TN-T and TN-I components change the band pattern of tropomyosin paracrystals formed in MgCl2 solutions, although in different ways. TN-T causes the formation of hexagonal net structures, double-stranded net or paracrystals which result from the collapse of the double-stranded net. TN-I at pH 7.9 causes the formation of paracrystals with a 400 A periodic band pattern and a 200 A repeat. The same band pattern can also be seen in tropomyosin paracrystals formed at pH values below 6.0.

3. The TN-C component does not precipitate tropomyosin in 0.1 M KCl. The aggregates of tropomyosin obtained with either TN-T or TN-I can be solubilized by the addition of TN-C. No interaction of TN-C was observed with tropomyosin paracrystals formed in the presence of MgCl2.


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