胎盘核心蛋白聚糖与胶原蛋白的亲和力。

Affinity of placental decorin for collagen.

作者信息

Batbayar T, Nomura Y, Ishii Y, Shirai K

机构信息

Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan.

出版信息

Biosci Biotechnol Biochem. 2000 Nov;64(11):2478-81. doi: 10.1271/bbb.64.2478.

DOI:10.1271/bbb.64.2478

PMID:11193421

Abstract

Decorin was isolated from 7 M 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 NH2-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.

摘要

通过离子交换和疏水色谱法从牛胎盘子叶的7M尿素提取物中分离出核心蛋白聚糖。通过SDS-PAGE分析，核心蛋白聚糖及其核心蛋白分别在约115 kDa处显示出一条宽带，在47 kDa处显示出一条单带。猪皮抗核心蛋白聚糖核心蛋白抗血清在蛋白质印迹法中与胎盘核心蛋白聚糖及其核心蛋白发生反应。胎盘子叶核心蛋白的NH2末端氨基酸序列与皮肤和骨骼核心蛋白的序列没有差异。通过在醋酸纤维素膜上进行电泳和软骨素酶消化率鉴定，核心蛋白聚糖的糖胺聚糖被确定为硫酸皮肤素。核心蛋白聚糖与III型、I型和V型胶原蛋白结合。