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The protein core of the largest proteoglycan monomer of articular cartilage. Gel electrophoretic pattern and tryptophanyl peptide bond cleavage.

作者信息

Stanescu V, Chaminade F, Muriel M P

机构信息

Unité de Recherches de Génétique Médicale (I.N.S.E.R.M. U.12), Hôpital des Enfants-Malades, Paris, France.

出版信息

Connect Tissue Res. 1987;16(4):377-84. doi: 10.3109/03008208709005622.

Abstract

The largest proteoglycan monomer of baboon (Papio papio) articular cartilage was isolated and the protein rich core was obtained after chondroitinase AC II and keratanase digestions. On SDS-PAGE the core yielded a single band with apparent Mr of 290,000. Tryptophanyl peptide bond cleavage of the core with N-chlorosuccinimide/urea gave 4 peptides with apparent Mr of 105,000, 66,000, 62,000 and 56,000

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