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Conformational Change of Glu-Plasminogen: Effects of N-Terminal Peptides of Glu-Plasminogen

  • Yumiko Takada
  • Tetsumei Urano
  • Satomi Takahashi
  • Kenji Sakakibara
  • Akikazu Takada
Conference paper

Abstract

Native plasminogen with glutamic acid at the N-terminus (Glu-plg) has a tight conformation possibly due to the binding of the N-terminal part to the lysine binding sites (LBS) on kringle 1 (1, 2) or kringle 4 (3) or kringle 5 through amino-hexyl (AH) site (4). Lysine analogues, therefore, could alter the conformation of Glu-plg to looser form (5, 6, 7) by dissociating the N-terminal peptides from LBS or AH site. Fig. 1 shows the schematic explanation of the conformation of Glu-plg and Lys-plg.

Keywords

Enhance Effect Tranexamic Acid Schematic Explanation Microtiter Plate Reader Exact Distance 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 1993

Authors and Affiliations

  • Yumiko Takada
    • 1
  • Tetsumei Urano
    • 1
  • Satomi Takahashi
    • 1
  • Kenji Sakakibara
    • 1
  • Akikazu Takada
    • 1
  1. 1.Department of PhysiologyHamamatsu University, School of MedicineHamamatsu, ShizuokaJapan

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