Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.4 (chondroitinase)
2,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Deglycosylation of bovine skin proteodermatan sulfate with chondroitinase ABC yielded a protein core with an apparent molecular weight of about 45,000. The amino acid sequence of this preparation was determined up to position 24. This region was enriched in acidic amino acids and proline compared with the whole protein core and it was predicted to be highly folded. The amino acid sequence determined in these experiments has a gap at position 4. Results obtained after beta-elimination-sulfite addition showed that residue 4 was an O-substituted hydroxyamino acid. The latter was identified as serine by sequencing the NH2-terminal region of the protein core (Mr approximately 43,000) isolated after a more complete deglycosylation of the proteoglycan with anhydrous HF. Serine 4 may be an attachment site for one of the few dermatan sulfate chains present in the proteoglycan.
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PMID:The NH2-terminal amino acid sequence of bovine skin proteodermatan sulfate. 665 8

Rat chondrosarcoma chondrocytes were cultured in the presence of puromycin to induce premature termination of core protein precursor. The structure and function of intracellular and extracellular proteoglycans were assessed by molecular sieve chromatography and polyacrylamide gel electrophoresis. [3H]Serine incorporation was maximally inhibited by 3 X 10(-4) M puromycin but unaffected by 10(-5) M puromycin. Proteoglycans synthesized in the presence of puromycin exhibited increased monomer size due to increased chondroitin sulfate chain size, typical of proteoglycans synthesized in the presence of protein synthesis inhibitors, but no loss in ability to bind to hyaluronic acid; and no loss in core protein size was observed after treatment with chondroitinase. These data suggest that chondrocytes select only completed or nearly completed core protein molecules to process into proteoglycans.
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PMID:Effect of puromycin on cartilage proteoglycan structure and capacity to bind hyaluronic acid. 671 56