Cartilage oligomeric matrix protein (COMP) is an abundant component of tendon

FEBS Lett. 1994 Nov 7;354(2):237-40. doi: 10.1016/0014-5793(94)01134-6.

Abstract

An abundant matrix protein was purified under native conditions from adult bovine tendon and identified as cartilage oligomeric matrix protein (COMP) by immunochemical crossreaction, amino acid sequence identity of tryptic peptides derived from both N- and C-terminal regions, and structure revealed by electron microscopy. Immunohistochemistry showed age-dependent differences in distribution of COMP in tendon.

Publication types

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

MeSH terms

  • Aging
  • Amino Acid Sequence
  • Animals
  • Cartilage, Articular / chemistry
  • Cattle
  • Extracellular Matrix Proteins
  • Glycoproteins*
  • Immunoenzyme Techniques
  • Matrilin Proteins
  • Membrane Proteins / analysis*
  • Membrane Proteins / chemistry
  • Membrane Proteins / ultrastructure
  • Microscopy, Electron
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / chemistry
  • Sequence Homology
  • Tendons / chemistry*
  • Trypsin

Substances

  • Extracellular Matrix Proteins
  • Glycoproteins
  • Matrilin Proteins
  • Membrane Proteins
  • Peptide Fragments
  • Trypsin