Production of 11 R ‐hydroxyeicosatetraenoic acid from arachidonic acid by Escherichia coli cells expressing arachidonate 11 R ‐lipoxygenase from Nostoc sp.

Author(s):  
Su‐Eun Kim ◽  
Tae‐Hun Kim ◽  
Min‐Ju Kim ◽  
Deok‐Kun Oh
2010 ◽  
Vol 13 (3) ◽  
pp. 129-133
Author(s):  
Ghusoon Ali Abdul Hasan Al-Sudany ◽  
◽  
Wasan Zuheir Majeed ◽  
Hind Jabbar Abdul Rhman Akram Al-Aubeidi ◽  
◽  
...  

2021 ◽  
Author(s):  
Cecile COURREGES ◽  
Mélanie Bonnecaze ◽  
Delphine Flahaut ◽  
Sophie Nolivos ◽  
Regis Grimaud ◽  
...  

A chemical fingerprint of Escherichia coli cells surface labeled by gelatin coated gold nanoparticles was obtained by combining Auger Electron Spectroscopy (AES) for single cell level chemical images, and Time-of-Flight...


1999 ◽  
Vol 276 (2) ◽  
pp. L280-L288 ◽  
Author(s):  
Elizabeth R. Jacobs ◽  
Richard M. Effros ◽  
John R. Falck ◽  
K. Malla Reddy ◽  
William B. Campbell ◽  
...  

Rabbit airway tissue is a particularly rich source of cytochrome P-4504A protein, but very little information regarding the effect(s) of 20-hydroxyeicosatetraenoic acid (20-HETE) on bronchial tone is available. Our studies examined the response of rabbit bronchial rings to 20-HETE and the metabolism of arachidonic acid and 20-HETE from airway microsomes. 20-HETE (10−8 to 10−6 M) produced a concentration-dependent relaxation of bronchial rings precontracted with KCl or histamine but not with carbachol. Relaxation to 20-HETE was blocked by indomethacin or epithelium removal, consistent with the conversion of 20-HETE to a bronchial relaxant by epithelial cyclooxygenase. A cyclooxygenase product of 20-HETE also elicited relaxation of bronchial rings. [14C]arachidonic acid was converted by airway microsomes to products that comigrated with authentic 20-HETE (confirmed by gas chromatography-mass spectrometry as 19- and 20-HETE) and to unidentified polar metabolites. [3H]20-HETE was metabolized to indomethacin-inhibitable products. These data suggest that 20-HETE is an endogenous product of rabbit airway tissue and may modulate airway resistance in a cyclooxygenase-dependent manner.


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