Semipreparative isolation of collagen types I, II, III and V by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electroelution

J Chromatogr A. 1997 Jan 17;758(2):313-8. doi: 10.1016/s0021-9673(96)00729-7.

Abstract

A simple method for the isolation of alpha-chains of different collagen types was developed. The procedure involves sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by electroelution of separated and defixed collagen alpha-chains. Collagen types I, II, III and V from different porcine tissues were recovered in high quantity (> 95%) and purity (> 98%) as evidenced by amino acid analysis. The procedure can be used for sample quantities smaller than required for conventional methods e.g. chromatographic procedures.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis*
  • Animals
  • Collagen / chemistry
  • Collagen / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel / methods*
  • Hydroxylysine / analysis
  • Hydroxyproline / analysis
  • Pepsin A / metabolism
  • Sodium Dodecyl Sulfate / chemistry*
  • Swine

Substances

  • Amino Acids
  • Hydroxylysine
  • Sodium Dodecyl Sulfate
  • Collagen
  • Pepsin A
  • Hydroxyproline