The partial amino acid sequence of bovine cartilage proteoglycan, deduced from a cDNA clone, contains numerous Ser-Gly sequences arranged in homologous repeats.

摘要: We have determined the sequence of a partial cDNA clone encoding C-terminal region bovine cartilage aggregating proteoglycan core protein. The deduced amino acid contains cysteine-rich which is homologous with chicken hepatic lectin. This lectin-homologous has previously been identified in rat and proteoglycan. presented here highly sequences this apparently globular region. A containing clusters Ser-Gly located N-terminal to lectin homology domain. These Ser-Gly-rich segments are arranged tandemly repeated, approx. 100-residue-long, domains. Each domain consists an 75-residue-long separated by 25-residue-long segment lacking dipeptides. dipeptides 10-residue-long 100-residue-long shorter repeated some six times each Serine residues these repeats potential attachment sites for chondroitin sulphate chains.