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Hydroxyproline and the Shrinkage Temperature of Collagen

Nature volume 196, pages 583–584 (1962)Cite this article

Abstract

WE did not discuss the suggestions1 based on the comparative shrinkage temperatures of various collagens since this aspect has been soundly criticized by Bowes and Moss2. In our investigations on infectious arthritis3,4 we purposely used untreated articular cartilage as a source of collagen in order to approach the conditions that exist in vivo, being fully aware that a greater thermal stability might exist for the reasons given by Dr. Rigby. Connective tissues (tendon, cartilage) not purified collagens were being compared on a per cent basis3. Both tissues were homogenized with tris buffer into fine suspensions according to the procedure of Schubert5. A comparison of bovine tendon and cartilage collagen in the presence of crystalline trypsin at different temperatures showed that tendon collagen was two to three tunes more solubilized than the cartilage collagen (unpublished observations).

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Authors and Affiliations

  1. Department of Surgery, Division of Orthopaedic Surgery, Western Reserve University School of Medicine, Cleveland, Ohio

    L. KLEIN

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  1. L. KLEIN
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KLEIN, L. Hydroxyproline and the Shrinkage Temperature of Collagen. Nature 196, 583–584 (1962). https://doi.org/10.1038/196583a0

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