title: Organization of collagen in the lyophilized cornea.
abstract: OBJECTIVE
  To investigate the organization of collagen fibrils in the lyophilized cornea.
  
  
  METHODS
  Freshly harvested porcine corneas (n = 10) were lyophilized and examined by synchrotron x-ray diffraction and transmission electron microscopy.
  
  
  RESULTS
  Collagen fibrils are highly compacted in lyophilized corneas. They become more widely spaced when the tissue is rehydrated, however, the distribution of imbibed water throughout the stroma is not necessarily homogeneous within an individual cornea, nor is it always similar in specimens that have been rehydrated to similar levels. In lyophilized corneas, the mean center-to-center interfibrilar spacing of the regularly arranged collagen reaches levels found in freshly thawed porcine corneas (between 74% and 78% water by weight) when between 74.3% and 81.6% of the rehydrated lyophilized cornea's weight is water.
  
  
  CONCLUSIONS
  Regularly arranged collagen fibrils are able to reapproximate their original spacings if lyophilized corneal tissue is rehydrated, although the manner in which imbibed water is distributed is somewhat unpredictable.
authors.affiliation: Anheuser-Busch Eye Institute, Department of Ophthalmology, Saint Louis University School of Medicine, MO 63104, USA.
authors.forename: A J
authors.initials: AJ
authors.lastname: Quantock
authors.forename: S M
authors.initials: SM
authors.lastname: Verity
authors.forename: D J
authors.initials: DJ
authors.lastname: Schanzlin
mesh_terms: D000818:Animals; D001834:Body Water; D003094:Collagen / Q000032:analysis* / Q000648:ultrastructure; D003315:Cornea / Q000737:chemistry* / Q000648:ultrastructure; D003319:Corneal Stroma / Q000737:chemistry / Q000648:ultrastructure; D003890:Desiccation; D008854:Microscopy, Electron; D013552:Swine; D014961:X-Ray Diffraction
chemical_list: D003094:Collagen