Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils

L. Y. Sakai, D. R. Keene, R. W. Glanville, H. P. Bachinger

Research output: Contribution to journalArticlepeer-review

227 Scopus citations

Abstract

Fibrillin, a connective tissue macromolecule (M(r) = 350,000) which is normally insoluble in its tissue form, has been purified from the medium of human skin fibroblast and ligament cells in culture. Analysis of the amino acid composition indicates that fibrillin contains approximately 14% cysteine, of which one-third appears to be in the free reactive sulfhydryl form. Electron microscopic images of fibrillin reveal an extended, flexible molecule approximately 148 nm long and 2.2 nm wide. These length measurements are consistent with shape calculations based upon velocity sedimentation data. It is likely that the material we have purified from cell culture medium represents monomeric fibrillin consisting of a single polypeptide chain. Additional ultrastructural immunohistochemical data presented here suggest a model for the parallel, head-to-tail alignment of fibrillin molecules in microfibrils.

Original languageEnglish (US)
Pages (from-to)14763-14770
Number of pages8
JournalJournal of Biological Chemistry
Volume266
Issue number22
StatePublished - Dec 1 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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