Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase

Nature ◽  
1991 ◽  
Vol 351 (6329) ◽  
pp. 714-718 ◽  
Author(s):  
David S. Bredt ◽  
Paul M. Hwang ◽  
Charles E. Glatt ◽  
Charles Lowenstein ◽  
Randall R. Reed ◽  
...  
Biochemistry ◽  
1992 ◽  
Vol 31 (29) ◽  
pp. 6627-6631 ◽  
Author(s):  
Kimberly A. White ◽  
Michael A. Marletta

1991 ◽  
Vol 1 (4) ◽  
pp. 86
Author(s):  
D.S. Bredt ◽  
P.M. Hwang ◽  
C.E. Glatt ◽  
C. Lowenstein ◽  
R.R. Reed ◽  
...  

1997 ◽  
Vol 272 (2) ◽  
pp. 977-983 ◽  
Author(s):  
Stephan K. Grant ◽  
Barbara G. Green ◽  
Regina Wang ◽  
Stephen G. Pacholok ◽  
John W. Kozarich

1997 ◽  
Vol 11 (6) ◽  
pp. 775-778
Author(s):  
J.B.G. Paquay ◽  
M.Ten Bolscher ◽  
H.-P. Voss ◽  
H. Timmerman ◽  
A. Bast

Author(s):  
Chi-Ming Wei ◽  
Margarita Bracamonte ◽  
Shi-Wen Jiang ◽  
Richard C. Daly ◽  
Christopher G.A. McGregor ◽  
...  

Nitric oxide (NO) is a potent endothelium-derived relaxing factor which also may modulate cardiomyocyte inotropism and growth via increasing cGMP. While endothelial nitric oxide synthase (eNOS) isoforms have been detected in non-human mammalian tissues, expression and localization of eNOS in the normal and failing human myocardium are poorly defined. Therefore, the present study was designed to investigate eNOS in human cardiac tissues in the presence and absence of congestive heart failure (CHF).Normal and failing atrial tissue were obtained from six cardiac donors and six end-stage heart failure patients undergoing primary cardiac transplantation. ENOS protein expression and localization was investigated utilizing Western blot analysis and immunohistochemical staining with the polyclonal rabbit antibody to eNOS (Transduction Laboratories, Lexington, Kentucky).


Sign in / Sign up

Export Citation Format

Share Document