期刊论文详细信息
FEBS Letters
The heparin‐binding site(s) of histidine‐rich glycoprotein as suggested by sequence homology with antithrombin III
Odani, Shoji1  Koide, Takehiko2  Foster, Donald2 
[1] Department of Biochemistry, Niigata University School of Medicine, Niigata 951, Japan;Department of Biochemistry, University of Washington, Seattle, WA 98195, USA
关键词: Histidine-rich glycoprotein;    Antithrombin III;    Heparin;    Heparin-binding site;    Sequence homology;   
DOI  :  10.1016/0014-5793(86)80092-8
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
PDF
【 摘 要 】

A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT HI is located. The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. These observations strongly suggest that the heparin-binding sites of HRG and AT III are evolutionarily related. There was no apparent sequence similarity between the remaining about 70% portions of the two proteins.

【 授权许可】

Unknown   

【 预 览 】
附件列表
Files Size Format View
RO201912020287532ZK.pdf 232KB PDF download
  文献评价指标  
  下载次数:12次 浏览次数:12次