Cell-free synthesis of cartilage proteins: partial identification of proteoglycan core and link proteins.
Cell-free synthesis of cartilage proteins: partial identification of proteoglycan core and link proteins.
复制标题
软骨蛋白的无细胞合成：蛋白聚糖核心和连接蛋白的部分鉴定。
DOI：
10.1021/bi00551a043
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发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
H. Mankin
中科院分区：
文献类型：
--
作者：
B. Treadwell;D. Mankin;P. Ho;H. Mankin
Benjamin V. Treadwell，* 大卫P. Mankin，Paul K. Ho和亨利J. Mankin摘要：从小牛关节软骨中分离的富含聚腺苷酸的RNA组分在软骨和小麦胚芽无细胞系统中翻译。放射性翻译产物被用来检测两种软骨蛋白的存在：蛋白聚糖核心和糖蛋白连接。这是通过利用两种蛋白质与透明质酸结合并形成足以在琼脂糖凝胶柱的空隙体积中聚集的聚集体的性质来实现的。当将含有透明质酸和连接物的小牛软骨提取物加入到软骨系统中合成的无细胞mRNA定向产物中并施加到Sepharose 6 B柱上时，回收了5-10%的放射性物质。关节软骨由分散在透明基质中的软骨细胞组成，所述透明基质由II型胶原和至少两种与透明质酸非共价结合的糖基化蛋白质形成。（Rosenberg，1978; Mankin，1970; Hascall，1977）。分子量为45 000-50 000的糖蛋白之一（蛋白聚糖连接）被认为稳定透明质酸和第二糖蛋白之间的相互作用，在此称为蛋白聚糖亚基[Mr（0.5-4.0）X 106]（Bonnet et al.，1978; Baker & Caterson，1978，1977; Keiser，1975; Oegema等人，1977; Caterson和Baker，1977; Swann等人，1976年）。亚基的蛋白质部分，称为核心[Mr（1.8-2.0）X 105]，仅占蛋白聚糖的10%，分子的大部分由硫酸化糖胺聚糖组成
Benjamin V. Treadwell,* David P. Mankin, Paul K. Ho, and Henry J. Mankin abstract: A poly (adenylic acid)-enriched RNA fraction isolated from calf articular cartilage was translated in cartilage and wheat germ cell-free systems. The radioactive translation products were assayed for thepresence of two cartilage proteins: proteoglycan core and glycoproteinlink. This was accomplished by utilizing the property both proteins have of binding to hyaluronic acidand forming an aggregate large enough to elute in the void volume of a Sepharose column. When an extract of calfcartilage, containing hyaluronic acid and link, was added to the cell-free mRNA directed products synthesized in a cartilage system and applied to a Sepharose 6B column, 5-10% of the radioactivematerial was recovered-/Articular cartilage consists of chondrocytes dispersed in a hyaline matrix formed by type II collagen and at least two glycosylated proteins noncovalently bound to hyaluronic acid (Rosenberg, 1978; Mankin, 1970; Hascall, 1977). One of the glycoproteins (proteoglycan link) of molecular weight 45 000-50 000 is believed to stabilize the interaction between hyaluronic acidand the second glycoprotein, referred to here as proteoglycan subunit [Mr (0.5-4.0) X 106](Bonnet et al., 1978; Baker & Caterson, 1978, 1977; Keiser, 1975; Oegema et al., 1977; Caterson & Baker, 1977; Swann et a}., 1976). The protein part of the subunit, known as core [Mr (1.8-2.0) X 105], constitutes only 10% of the proteoglycan with the bulk of the molecule consisting of the sulfated glycosaminoglycans