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首页> 外文期刊>The biochemical journal >Characterization of proteins from human synovium and mononuclear leucocytes that induce resorption of cartilage proteoglycan in vitro
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Characterization of proteins from human synovium and mononuclear leucocytes that induce resorption of cartilage proteoglycan in vitro

机译:人类滑膜和单核白细胞中诱导软骨蛋白聚糖吸收的蛋白质的表征

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pBoth human synovial tissue in culture and lectin-stimulated mononuclear leucocytes produced a protein that induced proteoglycan resorption in explants of bovine nasal cartilage and human articular cartilage. On gel filtration the protein had Mr 16000-20000 and on isoelectric focusing its pI was 5.2-5.3. The protein corresponded to catabolin, which has previously been identified as a product of cultured porcine synovial tissue and mononuclear leucocytes. The action of partially purified human catabolin was not inhibited by cortisol, although the activity of the leucocyte supernatants from which it had been isolated was inhibited. For this reason it is not possible to be sure that the active factor detected in the bioassay of the crude leucocyte culture supernatants is in fact catabolin./p
机译:>培养的人滑膜组织和受凝集素刺激的单核白细胞均产生一种蛋白,该蛋白在牛鼻软骨和人关节软骨的外植体中引起蛋白聚糖吸收。在凝胶过滤中,该蛋白的Mr为16000-20000,在等电聚焦时,其pI为5.2-5.3。该蛋白质对应于catabolin,后者先前已被鉴定为培养的猪滑膜组织和单核白细胞的产物。皮质醇不对部分纯化的人卡巴林的作用进行抑制,尽管从中分离出的白细胞上清液的活性受到抑制。因此,无法确定在白细胞培养上清液的生化分析中检测到的活性因子实际上是卡巴波林。

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