Summary
Specific antibodies against carp paravalbumin, crayfish calcium binding protein and crayfish arginine kinase were used for indirect immunofluorescence localization of the respective proteins. Simultaneous staining of the same muscle sections with human serum containing anti-actin autoantibodies served as a probe to identify the isotropic band.
Parvalbumin appears to be evenly distributed in carp white muscle. The crayfish calcium binding protein however shows a distinct localization, in the isotropic band, coincident with the actin staining. Arginine kinase, which has the same molecular weight and is extractible in the same way as the calcium binding protein, does not show this distinct localization, but is evenly present in crayfish tail muscle, similarly to parvalbumin.
The possible meaning of the different distribution of the two calcium binding proteins is discussed.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Benzonana, G., Cox, J.A., Kohler, L., Stein, E.A.: Caractérisation d'une nouvelle métalloprotéine calcique du myogène de certains crustacés. C.R. Acad Sci. (Paris) 279 D, 1491–1493 (1974b)
Benzonana, G., Kohler, L., Stein, E.A.: Regulatory proteins of crayfish tail muscle. Biochim. biophys. Acta (Amst.) 368, 247–258 (1974a)
Carafoli, E., Dabowska, R., Crovetti, F., Tiozzo, R., Drabikowski, W.: An in vitro study of the interaction of heart mitochondria with troponin-bound calcium. Biochem. biophys. Res. Commun. 62, 908–912 (1975)
Cebra, J.J., Goldstein, G.: Chromatographic purification of tetramethylrhodamine-immune globulin conjugates and their use in the cellular localization of rabbit γ-globulin polypeptide chains. J. Immunol. 95, 230–245 (1965)
Chaponnier, C., Kohler, L., Gabbiani, G.: Fixation of human antiactin autoantibodies on skeletal muscle fibers. Clin. exp. Immunol. (in press)
Collins, J.H.: Homology of myosin DTNB light chains with alkali light chains, troponin C and parvalbumin. Nature (Lond.) 259, 699–700 (1976)
Cox, J.A., Kohler, L., Benzonana, G.: Ionic composition and distribution of myogen proteins in the tail muscle of fresh water crayfish. Comp. Biochem. Physiol. 53 B, 101–105 (1976a)
Cox, J.A., Wnuk, W., Stein, E.A.: Isolation and properties of a sarcoplasmic calcium binding protein from crayfish. Biochemistry 15, 2613–2618 (1976b)
Eisenberg, E., Kielley, W.W.: Troponin-tropomyosin complex. Column chromatographic separation and activity of the three active troponin components with and without tropomyosin present. J. biol. Chem. 249, 4742–4748 (1974)
Fischer, E.H., Pocker, A., Saari, J.C.: The structure, function and control of glycogen phosphorylase. Essays Biochem. 6, 23–68 (1970)
Gabbiani, G., Ryan, G.B., Lamelin, J.P., Vassali, P., Majno, G., Bouvier, C.A. Cruchaud, A., Lüscher, E.F.: Human smooth muscle autoantibody: its identification as antiactin antibody and a study of its binding to “nonmuscular” cells. Amer. J. Path. 72, 473–488 (1973)
Gosselin-Rey, C.: Fish parvalbumins: immunochemical reactivity and biological distribution. In “Calcium-binding proteins” (Drabikowski, W., Strzelecka-Golaszewska, H., Carafoli, E., ed.), pp. 679–701. Amsterdam: Elsevier 1974
Harboe, N., Ingild, A.: Immunization, isolation of immunoglobulins, estimation of antibody titre. In. A manual of quantitative Immunoelectrophoresis (N.H. Axelsen, J. Krøll, B. Weeke, ed.), pp. 161–164. Oslo: Universitetsforlaget 1973
Hartshorne, D.J., Mueller, H.: The preparation of tropomyosin and troponin from natural actomyosin. Biochim. biophys. Acta (Amst.) 175, 301–319 (1969)
Kretsinger, R.H.: Calcium binding proteins. Ann. Rev. Biochem. 45, 239–266 (1976a)
Kretsinger, R.H.: Evolution and function of calcium binding proteins. Int. Rev. Cytol. 46, 323–393 (1976b)
Lehky, P., Blum, H.E., Stein, E.A., Fischer, E.H.: Isolation and characterization of parvalbumins from the skeletal muscle of higher vertebrates. J. biol. Chem. 249, 4332–4334 (1974)
Lehman, W., Szent-Györgyi, A.G.: Regulation of muscular contraction, Distribution of actin control and myosin control in the animal kingdom. J. gen. Physiol. 66, 1–30 (1975)
Lidman, K., Biberfeld, G., Fagraeus, A., Norberg, R., Tortenson, R., Utter, G. Anti-actin specificity of human smooth muscle antibodies in chronic active hepatitis. Clin. exp. Immunol. 24, 266–272 (1976)
Ouchterlony, Ö., Nilsson, L.Å. In: Handbook of experimental immunology, (D.M. Weir, ed), pp. 19.1–19.39. Oxford: Blackwell Scientific Publications 1974
Pechère, J.-F., Capony, J.-P., Demaille, J.: Evolutionary aspects of the structure of muscular parvalbumins. Syst. Zoology 22, 533–548 (1973)
Pechère, J.-F., Demaille, J., Capony, J.-P.: Muscular parvalbumins: preparative and analytical methods of general applicability. Biochim. biophys. Acta (Amst.) 236, 391–408 (1971)
Probst, E., Lüscher, E.F.: Studies on thrombosthenin A, the actin like moiety of the contractile protein from blood platelets. I. Isolation, characterization and evidence for two forms of thrombosthenin A. Biochim. biophys. Acta (Amst.) 278, 577–584 (1972)
Spudich, J.A., Watt, S.: The regulation of rabbit skeletal muscle contraction. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. biol. Chem. 246, 4866–4871 (1971)
Wnuk, W., Cox, J.A., Stein, E.A.: Structural changes induced by Ca++ and Mg++ in the calcium-binding protein from crayfish muscle. Abstract no 04-6-346 of the tenth International Congress of Biochemistry, Hamburg, 1976
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Benzonana, G., Wnuk, W., Cox, J.A. et al. Cellular distribution of sarcoplasmic calcium-binding proteins by immunofluorescence. Histochemistry 51, 335–341 (1977). https://doi.org/10.1007/BF00494370
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00494370