FEBS Letters | |
Stopped‐flow fluorescence kinetic studies of Glu‐plasminogen Conformational changes triggered by AH‐site ligand binding | |
Molgaard, Lone1  Christensen, Ulla1  | |
[1] Chemical Laboratory IV, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark | |
关键词: Stopped-flow fluorescence; Glu-plasminogen; AH-site; 6-Aminohexanoic acid; Conformational change: Plasminogen activation; | |
DOI : 10.1016/0014-5793(91)80117-L | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Binding of 6-aminohexanoic acid to the AH-site, a weak lysine binding site in Glu-plasminogen, alters the conformation of the molecule. The kinetics of the binding and the accompanying conformational change are investigated at pH 7.8. 25°C. Changes of intrinsic protein fluorescence were measured as a function of time after rapid mixing in a stopped-flow apparatus. The results reflect a two-step reaction mechanism: Rapid association of Glu-plasminogen and 6-aminohexanoic acid (K 1 = 44 mM) followed by the conformational change (k 2 = 69 g−1 and k −2 = 3 g−1) with on overall dissociation constant K 4 = 2.0 mM, Thus the conformational change is rather fast, t = 0.01 g. Its importance for the rates or Glu-plasminogen activation reactions is discussed.
【 授权许可】
Unknown
【 预 览 】
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