PMID: 2489642Jun 1, 1989Paper

Isolation and characterization of proteoglycan in bovine periodontal ligament

Kanagawa shigaku. The Journal of the Kanagawa Odontological Society
N Endo

Abstract

Proteoglycan, one of the major non-collagenous protein in the connective tissue, is bound with fibronectin and other cell adhesion proteins, and has a role in the formation of the tissue and the organ. Although the glycosaminoglycan components in various tissue have been widely investigated, the molecular structure of periodontal ligament proteoglycan (PDL-PG) was rarely reported. In present study, proteoglycans of bovine periodontal ligament were purified by chromatography from material adsorbed by DEAE-Sephacel from a guanidium HCl extract. The sequential chromatographic steps consisted of ion-exchange chromatography on DEAE-Sephacel in 4M urea and gel filtration on Sepharose CL-4B in 4M guanidium HCl. The preparation contained a relatively small proteoglycan (Mr = 132,000 dalton) and a free glycosaminoglycan chain (Mr = 88,000 dalton). A Mr = 58,000 dalton core protein was shown by gradient SDS gel electrophoresis after chondroitinase ABC or chondroitinase AC II treatment. The glycosaminoglycan chains after chondroitinase AC II hydrolysis were seen on gel as polydispersed, broad alcian blue staining material (Mr = 20,000-60,000 dalton) while chains were totally hydrolyzed by chondroitinase ABC. These indicate a chondroitin s...Continue Reading

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