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Characterization of the binding of [ 3 H]‐ l ‐N G ‐nitro‐arginine in rat brain
Author(s) -
Michel Anton D.,
Phul Ravinder K.,
Stewart Tracy L.,
Humphrey Patrick P.A.
Publication year - 1993
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1993.tb13566.x
Subject(s) - arginine , cytosol , nitric oxide synthase , nitroarginine , nitric oxide , biochemistry , chemistry , biology , enzyme , endocrinology , amino acid
In the present study tritiated l ‐N G ‐nitro‐arginine ( l ‐NOARG) has been shown to label specific binding sites in rat brain cytosol. We conclude that this ligand is directly labelling nitric oxide synthase (NOS). This conclusion is based on our observations (i) that binding was stereoselectively inhibited by l ‐arginine, in preference to d ‐arginine, and (ii) that a number of different NOS inhibitors were able to displace [ 3 H]‐ l ‐NOARG binding at similar concentrations to those required to inhibit the activity of rat brain cytosol NOS in functional studies.