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Electron microscope studies on collagen

III. Tryptic digestion of tropocollagen macromolecules

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Summary

The present paper describes the effect of intensive tryptic digestion of native tropocollagen (TC) macromolecules in solution. Contrary to earlier investigations it has been found that the trypsin treatment results in a fragmentation of the TC molecules. The addition of ATP to solutions exposed to the enzyme yields SLS fragments, 2250 Å in length. Comparison between these and normal SLS type aggregates shows that the scission occurs in a well-defined locus adjacent to the β-1/2-line seen after positive staining. The significance of this finding is discussed.

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References

  • Desnuelle, P.: Trypsin. In: The enzymes, ed. P. D. Boyer, H. Lardy and K. Myrbäck, pp. 119–132. New York and London: Academic Press 1960.

    Google Scholar 

  • Hodge, A. J., J. H. Highberger, G. G. J. Deffner and F. O. Schmitt: The effects of proteases on the tropocollagen macromolecule and on its aggregation properties. Proc. nat. Acad. Sci. (Wash.) 46, 197–206 (1960).

    Google Scholar 

  • Hodge, A. J., and J. A. Petruska: Some recent results on the electron microscopy of tropocollagen structures. In: Proc. of the fifth Internat. Congr. for Electron Microscopy, ed. S. S. Breese jr., vol. 2, p. QQ-1. New York and London: Academic Press 1962.

    Google Scholar 

  • , and F. O. Schmitt: Interaction properties of sonically fragmented collagen macromolecules. Proc. nat. Acad. Sci. (Wash.) 44, 418–424 (1958).

    Google Scholar 

  • : The charge profile of the tropocollagen macromolecule and the packing arrangement in native-type collagen fibrils. Proc. nat. Acad. Sci. (Wash.) 46, 186–197 (1960).

    Google Scholar 

  • Kühn, K., J. Kühn u. K. Hannig: Einwirkung von Trypsin auf gelöstes Kollagen. Hoppe-Seylers Z. physiol. Chem. 326, 50–60 (1961).

    Google Scholar 

  • Olsen, B. R.: Negative staining on various collagen structures. Paper presented at the Annual Meeting of the Scandinavian Electron Microscope Society, Uppsala, June 1962. Abstract in J. Ultrastruct. Res. 8, 190 (1963a).

    Google Scholar 

  • : Electron microscope studies on collagen. I. Native collagen fibrils. Z. Zellforsch. 59, 184–198 (1963b).

    Google Scholar 

  • : Electron microscope studies on collagen. II. Mechanism of linear polymerization of tropocollagen molecules. Z. Zellforsch. 59, 199–213 (1963c).

    Google Scholar 

  • Rich, A., and F. H. C. Crick: The molecular structure of collagen. J. molec. Biol. 3, 483–506 (1901).

    Google Scholar 

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This study was supported by grant NB-02215-04 from the National Institute of Neurological Diseases and Blindness, Public Health Service, U.S.A. and a Student research fellowship from the Norwegian Research Council for Science and the Humanities. This aid is gratefully acknowledged.

I am indebted to Mrs. J. Line Vaaland and Mr. B. V. Johansen for technical assistance.

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Olsen, B.R. Electron microscope studies on collagen. Zeitschrift für Zellforschung 61, 913–919 (1964). https://doi.org/10.1007/BF00340043

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  • DOI: https://doi.org/10.1007/BF00340043

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