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  • 标题:Origins of the specificity of tissue-type plasminogen activator
  • 本地全文:下载
  • 作者:L Ding ; G S Coombs ; L Strandberg
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1995
  • 卷号:92
  • 期号:17
  • 页码:7627-7631
  • DOI:10.1073/pnas.92.17.7627
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The role of subsite interactions in defining the stringent substrate specificity of tissue-type plasminogen activator (t-PA) has been examined by using an fd phage library that displayed random hexapeptide sequences and contained 2 x 10(8) independent recombinants. Forty-four individual hexapeptides were isolated and identified as improved substrates for t-PA. A peptide containing one of the selected amino acid sequences was cleaved by t-PA 5300 times more efficiently than a peptide that contained the primary sequence of the actual cleavage site in plasminogen. These results suggest that small peptides can mimic determinants that mediate specific proteolysis, emphasize the importance of subsite interactions in determining protease specificity, and have important implications for the evolution of protease cascades.
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