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The Qualitative and Quantitative Crosslink Chemistry of Collagen Matrices

  • Gerald L. Mechanic
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86)

Abstract

All normal mammalian collagen, whether it is from different fetal or mature tissues, exhibits the same physical chemical properties, such as shrinkage temperature, molecular weight, etc. Likewise, the protein fibrils, regardless of tissue origin, exhibit the same X-ray diffraction pattern and the same electron microscopic appearance. The amino acid compositions have characteristic contents, such as 1/3 glycine, approximately 1/3 imino acids, and in all, the combined hydroxylysine and lysine totals are the same. Some, however, vary in carbohydration and in the per cent of hydroxylation of the lysine; these hydroxylation variations are found in fetal tissues, mature bone and cartilage. In all cases, the collagen fibrils consist of collagen molecules arranged in a specific three dimensional array, although the collagen in the different tissues serve varied physiological functions. Despite the specific quarter-stagger configuration, another order of specificity might exist in each tissue collagen. This would direct the organization, packing and macromolecular stabilization (intermolecular covalent crosslinks) to specifically serve a tissue’s unique function.

Keywords

Aldehyde Lysine Fibril Apatite Crest 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1977

Authors and Affiliations

  • Gerald L. Mechanic
    • 1
  1. 1.Dental Research Center and Department of Biochemistry and NutritionUniversity of North CarolinaChapel HillUSA

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