Summary
The subunit composition, the thiol group content and the biological activities of cardiac tropomyosin (TM) of various animal species were compared. Cardiac TM from small animals such as rabbit, guinea-pig, rat and dog contain 2 SH/mole and were resolved into one band on SDS and acid urea electrophoresis and into two bands on alkaline urea electrophoresis. Chicken cardiac TM likewise gave one band and it contains 4 SH/mole. In contrast pig, sheep and human cardiac TM contain respectively 2.6, 2.4, and 2.4 SH/mole and were resolved into two bands α and β on the different electrophoresis systems used, with a β:α ratio respectively of I:4.2, I:4.6, I:4.8. The α-TM components from sheep skeletal and pig and sheep cardiac muscles were more positively charged than the rabbit skeletal α-TM component, as shown in alkaline urea electrophoresis system. The αα and αβ combinations of dimers found for skeletal muscle by other authors, were also found for cardiac pig TM.
All the TM have the same effect on the Ca2+-stimulated ATPase activity of desensitized actomyosin (DAM) and on the Mg2+-stimulated ATPase activity of DAM with troponin-complex.
This work suggests that the subunits of the TM from skeletal and cardiac muscles are heterogenous in their M.W. and their charges and that in the heart as well as in skeletal muscle a relationship seems to exist between the amount of the β component and the speed of contraction of the muscle: a higher amount of this component was found in the bulky hearts which are also those which contract slower.
Similar content being viewed by others
References
Akroyd, P.: Acrylamide gel slab electrophoresis in a simple glass cell for improved resolution and comparison of serum proteins. Analyt. Biochem.19, 399–410 (1967)
Anfinsen, C. B., Haber, E.: Studies on the reduction and reformation of protein disulfide bonds. J. biol. Chem.236, 1361–1363 (1961)
Bailey, J. L.: Miscellaneous analytical methods: estimation of protein. In: Techniques in protein chemistry, p. 341. Second edition. Amsterdam: Elsevier 1967
Bailey, K.: Tropomyosin: a new asymmetric protein component of the muscle fibril. Biochem. J.43, 271–279 (1948)
Barany, M.: ATPase activity of myosin correlated with speed of muscle shortening. J. gen. Physiol.50, 197–216 (1967)
Besse, P., Bricaud, H.: Moyens d'étude de la performance cardiaque chez l'homme. Rev. Prat.22, 2911–2931 (1972)
Bodwell, C. E.: Two subunits of Tropomyosin B. Arch. Biochem. Biophys.122, 246–261 (1967)
Chowrashi, P., Kaldor, G.: Studies on the electrophoretic mobility of troponin in the presence of Ca2+, Mg2+ and Mg-ATP. Proc. Soc. exp. Biol. (N. Y.)133, 969–972 (1970)
Close, R. I.: Dynamic properties of mammalian skeletal muscles. Physiol. Rev.52, 129–197 (1972)
Cohen, C., Caspar, D. L., Johnson, J. P., Nauss, K., Margossian, S. S., Parry, D. A. D.: Tropomyosin-troponin assembly. Cold Spr. Harb. Symp. quant. Biol.37, 287–297 (1973)
Crestfield, A. M., Moore, S., Stein, W. H.: The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. biol. Chem.238, 622–627 (1963)
Crick, F. H. C.: The packing of α-helices: simple coiled-coils. Acta crystallogr.6, 689 (1953)
Cummins, P., Perry, S. V.: The subunits and biological activity of polymorphic forms of tropomyosin. Biochem. J.133, 765–777 (1973)
Cummins, P., Perry, S. V. Chemical and immunochemical characteristics of tropomyosins from striated and smooth muscle. Biochem. J.141, 43–49 (1974)
Davies, A. S., Gunn, H. M.: A comparative histochemical study of the mammalian diaphragm and semitendinosus. J. Anat. (Lond.)110, 137–139 (1971)
Davies, A. S., Gunn, H. M.: Histochemical fibre types in the mammalian diaphragm. J. Anat. (Lond.)112, 41–60 (1972)
Delcayre, C., Swynghedauw, B. A comparative study of heart myosin ATPase and light subunits from different species. Pflügers Arch.355, 39–47 (1975)
Drabikowski, W., Novak, E.: Thiol group content in tropomyosin and troponin. Acta biochim. pol.17, 221–229 (1970)
Ebashi, S., Wakabayashi, T., Ebashi, F. Troponin and its components. J. Biochem.69, 441–445 (1971)
Eisenberg, E., Kielley, W. W.: Troponin-tropomyosin complex. J. biol. Chem.249, 4742–4746 (1974)
Flavin, M.: Microbial transsulfuration: the mechanism of an enzymatic disulfide elimination reaction. J. biol. Chem.237, 768–777 (1962)
Habeeb, A. F. S. A.: A sensitive method for localization of disulfide containing peptides in column effluents. Analyt. Biochem.56, 60–65 (1973)
Hartshorne, D. J., Mueller, H.: The preparation of tropomyosin and troponin from natural actomyosin. Biochim. biophys. Acta (Amst.)175, 301–319 (1969)
Henderson, A. H., Craig, R. J., Sonnenblick, E. H., Urschel, C. W.: Species differences in intrinsic myocardial contractility. Proc. Soc. exp. Biol. (N. Y.)134, 930–932 (1970)
Hodges, R. S., Smillie, L. B.: Chemical evidence for chain heterogeneity in rabbit muscle tropomyosin. Biochem. biophys. Res. Commun.41, 987–994 (1970)
Johnson, L. S.: Non-identical tropomyosin subunits in rat skeletal muscle. Biochim. biophys. Acta (Amst.)371, 219–225 (1974)
Katz, A. M.: Contractile proteins of the heart. Physiol. Rev.50, 63–158 (1970)
Klotz, C., Aumont, M. C., Léger, J. J., Swynghedauw, B.: Human cardiac myosin ATPase and light subunits. A comparative study. Biochim. biophys. Acta (Amst.)386, 461–469 (1975)
Klotz, C., Berson, G., Swynghedauw, B.: Etude des proteines myofibrillaires par electrophorèse sur gel de polyacrylamide en présenee d'urée ou de SDS. Ann. Biol. Clin.31, 413–419 (1973)
Noelken, M., Holtzer, A. M.: The denaturation of paramyosin and tropomyosin by guanidine hydrochloride. In: Biochemistry of muscle contraction (J. Gergely, ed.), p. 374. Boston: Little, Brown and Co. 1964
Perrie, W. T., Perry, S. V.: An electrophoretic study of the low molecular weight components of myosin. Biochem. J.119, 31–38 (1970)
Potter, J. D., Gergely, J.: Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction. Biochemistry13, 2697–2703 (1974)
Samaha, F. J.: Tropomyosin and troponin in normal and dystrophic human muscle. Arch. Neurol. (Chic.)26, 547–550 (1972)
Schaub, M. C., Perry, S. V.: The relaxing protein system of striated muscle. Resolution of the troponin-complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin. Biochem. J.115, 993–1004 (1969)
Schaub, M. C., Perry, S. V., Hartshorne, D. J.: The effect of tropomyosin on the adenosine triphosphatase activity of desensitized actomyosin. Biochem. J.105, 1235–1243 (1967)
Sender, P. M.: Muscle fibrils: solubilization and gel electrophoresis. FEBS Letters17, 106–110 (1971)
Sodek, J., Hodges, R. S., Smillie, L. B., Jurasek, L.: Aminoacid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc. nat. Acad. Sci. (Wash.)69, 3800–3804 (1972)
Syrovy, I.: (Abstract) Properties of cardiac and skeletal myosin from mammals differing in size. International Symposium on Adaptability of Cardiac Muscle. Prague, June 12–14 (1974)
Syrovy, I., Gutman, E., Melichna, J.: Differential responses of myosin ATPase activity and contraction properties of fast and slow rabbit muscles following denervation. Experientia (Basel)27, 1426–1427 (1971)
Swynghedauw, B., Bouveret, P., Piguet, V.: Le dosage du phosphore en présence d'adénosine-triphosphate. Ann. Biol. Clin.28, 159–163 (1970)
Weber, K., Osborn, M.: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. biol. Chem.244, 4406–4412 (1969)
Wikman-Coffelt, J., Fenner, C., Smith, A., Mason, D. T.: Comparative analyses of the kinetics and subunits of myosins from canine skeletal muscle and cardiac tissue. J. biol. Chem.250, 1257–1262 (1975)
Wilkinson, J. M., Perry, S. V., Cole, H. A., Trayer, I. P.: The regulatory proteins of the myofibril separation and biological activity of the component of inhibitory-factor preparations. Biochem. J.127, 215–228 (1972)
Woods, E. F.: Comparative physicochemical studies on vertebrate tropomyosins. Biochemistry8, 4336–4344 (1969)
Yasui, B., Fuchs, F., Briggs, F. N.: The role of the sulfhydryl groups of tropomyosin and troponin in the calcium control of actomyosin contractility. J. biol. Chem.243, 735–742 (1968)
Yazaki, Y., Raben, M. S.: Cardiac myosin adenosine triphosphatase of rat and mouse: distinctive enzymatic properties compared with rabbit and dog cardiac myosin. Circulat. Res.35, 15–23 (1974)
Note added in proof Since this paper was submitted Ookubo et al. (1975) have also reported the presence of a β cardiac component of tropomyosin in a bulky heart (bovine).
Ookubo, N., Ueno, H., Ooi, T.: Similarities and differences of the α and β components of tropomyosin. J. Biochem.78, 739–747 (1975).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Leger, J., Bouveret, P., Schwartz, K. et al. A comparative study of skeletal and cardiac tropomyosins. Pflugers Arch. 362, 271–277 (1976). https://doi.org/10.1007/BF00581181
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00581181