Link protein interactions with hyaluronate and proteoglycans. Characterization of two distinct domains in bovine cartilage link proteins.
Hyaluronic acid-binding region and trypsin-link protein were prepared from bovine nasal cartilage proteoglycan complex after trypsin digestion. Binary complexes were reformed between trypsin-link protein and hyaluronic acid-binding region or hyaluronate. Upon trypsin treatment of these complexes, two fragments deriving from trypsin-link protein were characterized. One of them, of 20 kDa, corresponds in fact to a 140-amino acid long fragment and bears the glycosylated site of trypsin-link protein; it appears to be involved in proteoglycan/link protein interaction. The other, of 22 kDa, corresponds to the 200 C-terminal amino acids of trypsin-link protein; it appears to be involved in the binding of link protein with hyaluronic acid. A structural model of bovine trypsin-like protein depicting two distinct domains involved in hyaluronate and proteoglycan subunit interactions is proposed.
Périn
J P
JP
Laboratory of Proteins, University of Paris V, France.
Bonnet
F
F
Thurieau
C
C
Jollès
P
P
D000818:Animals; D002356:Cartilage / Q000378:metabolism*; D002417:Cattle; D002850:Chromatography, Gel; D016326:Extracellular Matrix Proteins; D006820:Hyaluronic Acid / Q000378:metabolism*; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism*; D011509:Proteoglycans / Q000378:metabolism*; D014357:Trypsin; D000099249:Proteoglycan Link Protein
D016326:Extracellular Matrix Proteins; D006820:Hyaluronic Acid; D046911:Macromolecular Substances; D010446:Peptide Fragments; D011506:Proteins; D011509:Proteoglycans; D014357:Trypsin; D000099249:Proteoglycan Link Protein