These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Fluorescence spectrophotometric studies on the conformational changes induced by omega-aminoacids in two isozymes of Glu-plasminogen (I and II).
    Author: Takada A, Takada Y, Sugawara Y.
    Journal: Thromb Res; 1984 Mar 01; 33(5):461-9. PubMed ID: 6719394.
    Abstract:
    Glu-plasminogen I (Glu-plg I: with two carbohydrate chains) and Glu-plg II (with one carbohydrate chain) were separated by a gradient elution of 6 aminohexanoic acid (6AHA) through lysine-Sepharose. Each preparation was excited with ultraviolet light of wave length at 291 nm. The intensity of fluorescence was measured at 340 nm. The intensity of fluorescence increased to a small extent at 0.02 mM of tranexamic acid (t-x) for Glu-plg I and then quickly increased from 0.1 mM of t-x to reach the peak at 0.6 mM. The intensity of fluorescence for Glu-plg II started to increase at 0.2 mM to reach the peak at 0.7 mM. No small increase of fluorescence was observed at less than 0.2 mM of t-x for Glu-plg II. Kdobs of Glu-plg I for t-x and 6AHA were 0.34 mM and 1.35 mM, respectively, whereas Kdobs of Glu-plg II for t-x and 6AHA were 0.46 mM and 3.3 mM, respectively. When Glu-plg I and II were activated by urokinase (UK) and the hydrolysis of S-2251 was measured, the extent of hydrolysis increased in the presence of t-x and 6AHA. The rate of the increase of S-2251 hydrolysis (thus activation rate of Glu-plg I and II with UK) increased in parallel with increase in fluorescence intensity of Glu-plg I and II in the presence of omega-aminoacids. In conclusion, changes in the activation rate with UK and in fluorescence intensity were observed at lower concentrations of omega-aminoacids for Glu-plg I than for Glu-plg II.
    [Abstract] [Full Text] [Related] [New Search]