Elastin purification and solubilization

Methods Cell Biol. 2018:143:207-222. doi: 10.1016/bs.mcb.2017.08.012. Epub 2017 Nov 6.

Abstract

The functional form of elastin is a highly cross-linked polymer that organizes as sheets or fibers in the extracellular matrix. Purification of the mature protein is problematic because its insolubility precludes its isolation using standard wet-chemistry techniques. Instead, relatively harsh experimental approaches designed to remove nonelastin "contaminates" are employed to generate an insoluble product that has the amino acid composition expected of elastin. Although soluble, tropoelastin also presents problems for isolation and purification. The protein's extreme stickiness and susceptibility to proteolysis require careful attention during purification and in tropoelastin-based assays. This chapter describes the most common approaches for purification of elastin and for preparing solubilized forms of the protein.

Keywords: Cross-links; Desmosine; Elastic fiber; Elastin; Microfibril.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkalies / chemistry
  • Animals
  • Elastin / analysis
  • Elastin / chemistry
  • Elastin / isolation & purification*
  • Elastin / ultrastructure
  • Extracellular Matrix / chemistry*
  • Extracellular Matrix / ultrastructure
  • Hot Temperature
  • Microscopy, Electron
  • Molecular Imaging / instrumentation
  • Molecular Imaging / methods*
  • Proteolysis
  • Solubility
  • Staining and Labeling / instrumentation
  • Staining and Labeling / methods*

Substances

  • Alkalies
  • Elastin