首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites
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Murine betaglycan primary structure, expression and glycosaminoglycan attachment sites

机译:鼠β聚糖的一级结构,表达和糖胺聚糖附着位点

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The primary structure of murine betaglycan, also known as transforming growth factor beta (TGF-β) type III receptor, was deduced from the nucleotide sequence of a cDNA clone isolated from a heart library. Murine betaglycan is a single spanning membrane polypeptide of 850 amino acids which is highly similar to betaglycan of other species. Transfection of this cDNA into COS1 cells resulted in the expression of a membrane proteoglycan that binds TGF-β and is recognized by antibodies raised against rat betaglycan. COS1 cells transfected with the double mutant Ser533Ala; Ser544Ala of the murine betaglycan cDNA produced a TGF-β type III receptor devoid of glycosaminoglycan chains.
机译:鼠β聚糖的一级结构,也称为转化生长因子β(TGF-β)III型受体,是从从心脏文库中分离的cDNA克隆的核苷酸序列推导的。鼠β聚糖是具有850个氨基酸的单跨膜多肽,与其他物种的β聚糖高度相似。将该cDNA转染到COS1细胞中,导致膜蛋白聚糖的表达,该蛋白聚糖结合TGF-β并被针对大鼠β聚糖的抗体所识别。用双突变体Ser533Ala转染的COS1细胞;鼠β聚糖的Ser544Ala产生了没有糖胺聚糖链的TGF-βIII型受体。

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