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Aggregated proteoglycan synthesis in organ cultures of human nucleus pulposus
Ist Teil von
The Journal of biological chemistry, 1979-11, Vol.254 (21), p.10579-10581
Ort / Verlag
United States: American Society for Biochemistry and Molecular Biology
Erscheinungsjahr
1979
Quelle
MEDLINE
Beschreibungen/Notizen
Proteoglycans isolated under associative conditions in the presence of protease inhibitors from human nucleus pulposus contained
17% aggregate and 83% non-aggregating monomer (Kav = 0.5 on Sepharose CL-2B). Isolated aggregate after reduction and alkylation
was resolved into two components (Kav = 0.15 and 0.43) on Sepharose CL-2B. Labeled proteoglycans isolated from parallel samples
pulsed with [35S]sulfate and chased for up to 18 h were present largely as aggregated material (up to 78%). Reduction and
alkylation of the labeled samples gave a labeled proteoglycan monomer with Kav = 0.15. Both the labeled and unlabeled chondroitin
sulfate chains had the same distribution on Sepharose CL-6B and equivalent molecular weights (Mr = 2.0 x 10(3)). After chondroitinase
ABC digestion, the unlabeled keratan sulfate-protein core was polydisperse with a Kav = 0.38 on Sepharose CL-4B while the
labeled keratan sulfate-protein core had a Kav = 0.05. This indicates that the newly synthesized proteoglycan had a large
core protein and suggests that the proteoglycans present in nucleus pulposus are originally synthesized as large molecular
weight, aggregating proteoglycans.