Influence of sugar chain on fibrin affinity of recombinant t-PA

Shoichi Aoki, Norihide Shimizu, Manabu Shimonishi, Masaru Kitagawa, Kazuo Okumura, Yusuke Tanigawara

Research output: Contribution to journalArticle

3 Citations (Scopus)


The role of the sugar chain on the fibrin affinity property of tissue plasminogen activator (t-PA) was investigated using two variants of wild type t-PA (WT t-PA I and WT t-PA II) and mutant type t-PA (mt-PA ; Gln117 t-PA I and Gln117 t-PA II), whose sugar chains have different structures. In terms of fibrin affinity, Gln117 t-PA was higher than WT t-PA ; moreover, Type II was higher than Type I. Bindings mediated via finger domain (F mode) and kringle 2 domain (K2 mode) were distinguished using ε-amino caproic acid (EACA). Consequently, F mode and K2 mode bindings were inhibited by the sugar chains at Asn117 and 184, respectively. These results were assumed to be due to the steric hindrance of the sugar chains.

Original languageEnglish
Pages (from-to)295-298
Number of pages4
JournalBiological and Pharmaceutical Bulletin
Issue number3
Publication statusPublished - 2001 Apr 5


  • Gln117 t-PA
  • Tissue plasminogen activator
  • Variant
  • ε-amino caproic acid

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science

Fingerprint Dive into the research topics of 'Influence of sugar chain on fibrin affinity of recombinant t-PA'. Together they form a unique fingerprint.

  • Cite this