Summary
The present paper describes an electron microscope investigation of the structure of fibrous-long-spacing (FLS) and segment-long-spacing (SLS) tropocollagen aggregates. Moreover, the mechanism of linear polymerization of tropocollagen (TC) molecules to protofibrils is dealt with.
Evidence of overlapping of the TC molecules by about 500 Å in various types of FLS is presented. No observations in favor of molecular end-to-end aggregation and existence of tail-peptides involved in such aggregation were made.
It is claimed that in native fibrils a molecular overlapping of about 300 Å exists. The zone of overlap corresponds to the band defined in earlier literature. This finding is consistent with the observation of Hodge and Petruska (1962) that the length of the TC molecule exceeds that of four periods of native type fibrils by about 10%.
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This study was supported by grant B-2215 from the National Institute of Neurological Diseases and Blindness, Public Health Service, U.S.A. This aid is gratefully acknowledged.
The author was supported by a Student research fellowship from the Norwegian Research Council for Science and the Humanities.
I am indebted to Mrs. J. L. Vaaland, Mr. B. V. Johansen and Mr. E. Risnes for technical assistence. Particular thanks are due to Prosector T. W. Blackstad, M. D., for his continued support and great interest in the work and for his kind assistence in preparing the manuscript.
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Olsen, B.R. Electron microscope studies on collagen. Z. Zellforsch. 59, 199–213 (1963). https://doi.org/10.1007/BF00320445
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DOI: https://doi.org/10.1007/BF00320445