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连接蛋白cDNA序列揭示了一种串联重复的蛋白质结构。

Link protein cDNA sequence reveals a tandemly repeated protein structure.

作者信息

Doege K, Hassell J R, Caterson B, Yamada Y

出版信息

Proc Natl Acad Sci U S A. 1986 Jun;83(11):3761-5. doi: 10.1073/pnas.83.11.3761.

Abstract

Link protein stabilizes the cartilage proteoglycan/hyaluronic acid aggregate by binding to both components. We screened a cDNA library prepared from rat chondrosarcoma mRNA in the lambda gt11 expression vector with monoclonal antibodies and polyclonal antisera to link protein. We obtained a clone for two-thirds of the link protein cDNA and identified it based on its deduced amino acid sequence. There are four RNA transcripts for link protein, ranging from 1.5 to 5.5 kilobases in size. The deduced amino acid sequence for link protein shows two domains of 100 residues each, which share 44% homology; within each domain is a 19-residue stretch 74% homologous with its counterpart. This structure indicates that link protein may have been formed by gene duplication.

摘要

连接蛋白通过与软骨蛋白聚糖和透明质酸这两种成分结合来稳定软骨蛋白聚糖/透明质酸聚集体。我们用针对连接蛋白的单克隆抗体和多克隆抗血清筛选了在λgt11表达载体中由大鼠软骨肉瘤mRNA制备的cDNA文库。我们获得了三分之二的连接蛋白cDNA克隆,并根据其推导的氨基酸序列对其进行了鉴定。连接蛋白有四种RNA转录本,大小在1.5至5.5千碱基之间。连接蛋白推导的氨基酸序列显示出两个各含100个残基的结构域,它们具有44%的同源性;每个结构域内有一段19个残基的序列,与对应序列有74%的同源性。这种结构表明连接蛋白可能是通过基因复制形成的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d92/323603/37cf299275f1/pnas00315-0203-a.jpg

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