Affinity of Placental Decorin for Collagen
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概要
- 論文の詳細を見る
Decorin was isolated from 7M urea extract of bovine placental cotyledons by ion-exchange and hydrophobic chromatography. Decorin and its core protein showed a broad band at about 115 kDa and a single band at 47 kDa, respectively by SDS-PAGE. Anti-decorin core protein antiserum from pig skin was reacted with placental decorin and its core protein in western blotting. The NH_2-terminal amino acid sequence of core protein from placental cotyledons was not different from that of core protein from skin and bone. Glycosaminoglycan of decorin was identified as dermatan sulfate by electrophoresis on a cellulose-acetate membrane and chondroitinase digestivity. Decorin bound to collagen in the order for type III, I, and V.
- 社団法人日本農芸化学会の論文
- 2000-11-23
著者
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Nomura Y
Biotechnology Research Laboratories Takara Shuzo Co. Ltd.
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Ishii Yasuhiro
Faculty Of Agriculture Tokyo University Of Agriculture And Technology
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白井 邦郎
Faculty Of Agriculture Tokyo University Of Agriculture And Technology
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Ishii Y
Faculty Of Agriculture Tokyo University Of Agriculture And Technology
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NOMURA Yoshihiro
Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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ISHII Yasuhiro
Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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SHIRAI Kunio
Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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BATBAYAR Tumurbaatar
Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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Nomura Yoshihiro
Applied Protein Chemistry Agri. Tokyo Univ. Agri. And Tech.
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Batbayar Tumurbaatar
Applied Protein Chemistry Faculty Of Agriculture Tokyo University Of Agriculture And Technology
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