Molecular structure, processing, and tissue distribution of matrilin-4.

@article{Klatt2001MolecularSP,
  title={Molecular structure, processing, and tissue distribution of matrilin-4.},
  author={Andreas R. Klatt and Dirk Nitsche and Birgit Kobbe and Marcus Macht and Mats Paulsson and Raimund Wagener},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 20},
  pages={17267-75}
}
Matrilin-4 is the most recently identified member of the matrilin family of von Willebrand factor A-like domain containing extracellular matrix adapter proteins. Full-length matrilin-4 was expressed in 293-EBNA cells, purified using affinity tags, and subjected to biochemical characterization. The largest oligomeric form of recombinantly expressed full-length matrilin-4 is a trimer as shown by electron microscopy, SDS-polyacrylamide gel electrophoresis, and mass spectrometry. Proteolytically… CONTINUE READING