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Cartilage oligomeric matrix protein (COMP) is an abundant component of tendon
Author(s) -
DiCesare Paul,
Hauser Nik,
Lehman Daniel,
Pasumarti Subhalakshmi,
Paulsson Mats
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01134-6
Subject(s) - cartilage oligomeric matrix protein , tendon , cartilage , immunohistochemistry , matrix (chemical analysis) , chemistry , electron microscope , n terminus , peptide sequence , microbiology and biotechnology , biochemistry , anatomy , pathology , biology , medicine , osteoarthritis , chromatography , gene , optics , physics , alternative medicine
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.

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