The N-terminal sequence of the large proteoglycan of articular cartilage.
A peptide with hyaluronic acid-binding properties was isolated from trypsin digests of bovine articular cartilage proteoglycan aggregate. This peptide originated from the N-terminus of the proteoglycan core protein, retained its function of forming complexes with hyaluronate and link protein and contained at least one keratan sulfate chain. Amino acid sequence data demonstrated that the first six amino acid residues of the N-terminus of bovine articular cartilage proteoglycan core protein differed from the same region from the rat chondrosarcoma proteoglycan. Further sequence data indicate areas of considerable sequence homology in the hyaluronic acid-binding regions of proteoglycans from the two species.
Ilic
M Z
MZ
Department of Biochemistry, Monash University, Clayton, Victoria, Australia.
Handley
C J
CJ
Robinson
H C
HC
D000595:Amino Acid Sequence; D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry*; D002417:Cattle; D006820:Hyaluronic Acid / Q000378:metabolism; D008969:Molecular Sequence Data; D011509:Proteoglycans / Q000737:chemistry* / Q000378:metabolism; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin / Q000378:metabolism
D011509:Proteoglycans; D006820:Hyaluronic Acid; D014357:Trypsin