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X-Ray Analysis of Enzymically Purified Elastin from Bovine Ligamentum Nuchae

  • A. Serafini-Fracassini
  • J. M. Field
  • B. Delf
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 79)

Abstract

Insoluble elastin has been isolated from bovine 1igamentum nuchae by treatment with guanidine and dithiothreitol followed by digestion with collagenase, purified by affinity chromatography. The preparation was subjected to both wide- and low-angle X-ray analysis. The wide-angle diffraction patterns of relaxed and stretched specimens showed only two broad diffraction rings, corresponding to spacings of 4.5 and 9.3 Å. No significant reflections were visible in the low-angle diffraction pattern of unstretched specimens, but on stretching an equatorial reflection was produced, corresponding to spacings of between 45 and 50 Å.

Keywords

Significant Reflection Equatorial Reflection Fibrous Protein Regular Secondary Structure Meridional Reflection 
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

© Plenum Press, New York 1977

Authors and Affiliations

  • A. Serafini-Fracassini
    • 1
  • J. M. Field
    • 1
  • B. Delf
    • 2
  1. 1.Department of BiochemistryUniversity of St. AndrewsSt. AndrewsScotland
  2. 2.Department of PhysicsUniversity CollegeCardiffUK

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