Purification and Characterization of Two Fibrinolytic Enzymes from a Marine Green Alga, Codium intricatum

Author(s):  
Kiminori Matsubara ◽  
Hiroyuki Sumi ◽  
Kanji Hori ◽  
Keisuke Miyazawa
2010 ◽  
Vol 23 (4) ◽  
pp. 745-753 ◽  
Author(s):  
Jong Won Han ◽  
Kang Sup Yoon ◽  
Tatyana A. Klochkova ◽  
Mi-Sook Hwang ◽  
Gwang Hoon Kim

2006 ◽  
Vol 0 (0) ◽  
pp. 060609080250009-??? ◽  
Author(s):  
Gwang Hoon Kim ◽  
Tatyana A. Klochkova ◽  
Kang-Sup Yoon ◽  
Yoon-Sup Song ◽  
Key Pyoung Lee

2011 ◽  
Vol 46 (5) ◽  
pp. 1212-1215 ◽  
Author(s):  
Fei Yan ◽  
Zhaoan Chen ◽  
Wei Li ◽  
Xupeng Cao ◽  
Song Xue ◽  
...  

FEBS Letters ◽  
1999 ◽  
Vol 443 (2) ◽  
pp. 144-148 ◽  
Author(s):  
Yoshiyuki Ueno ◽  
Norihide Kurano ◽  
Shigetoh Miyachi

2014 ◽  
Vol 123 (1) ◽  
pp. 61-76 ◽  
Author(s):  
Xiaochun Qin ◽  
Wenda Wang ◽  
Lijing Chang ◽  
Jinghua Chen ◽  
Peng Wang ◽  
...  

1997 ◽  
Vol 52 (11-12) ◽  
pp. 740-746 ◽  
Author(s):  
Röbbe Wünschiers ◽  
Thomas Zinn ◽  
Dietmar Linder ◽  
Rüdiger Schulz

Abstract Purification of a soluble cytochrome c6 from the unicellular green alga Scenedesmus obliquus by a simple and rapid method is described. The purification procedure includes ammonium sulfate precipitation and non-denaturating PAGE. The N-terminal sequence of the first 20 amino acids was determined and shows 85% similarity and 75% identity to the sequence of cytochrome c6 from the green alga Monoraphidium braunii. The ferrocyto-chrome shows typical UV/VIS absorption peaks at 552.9, 521.9 and 415.7 nm. The apparent molecular mass was estimated to be 12 kD a by SDS-PAGE. EPR-spectroscopy at 20K shows resonances indicative for two distinct low-spin heme forms.


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