Arginase activity in mitochondria – An interfering factor in nitric oxide synthase activity assays

Author:

Venkatakrishnan Priya,Nakayasu Ernesto S.,Almeida Igor C.,Miller R.T.

Funder

National Institute of Environmental Health Sciences (NIEHS)/NIH

National Center for Research Resources (NCRR)/NIH

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference39 articles.

1. Absence of nitric-oxide synthase in sequentially purified rat liver mitochondria;Venkatakrishnan;J. Biol. Chem.,2009

2. Endothelium-derived nitric oxide: actions and properties;Ignarro;FASEB J.,1989

3. Endothelium-derived relaxing factor and nitric oxide possess identical pharmacologic properties as relaxants of bovine arterial and venous smooth muscle;Ignarro;J. Pharmacol. Exp. Ther.,1988

4. Endothelium-derived relaxing and contracting factors;Furchgott;FASEB J.,1989

5. Calmodulin-dependent endothelium-derived relaxing factor/nitric oxide synthase activity is present in the particulate and cytosolic fractions of bovine aortic endothelial cells;Forstermann;Proc. Natl. Acad. Sci. USA,1991

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