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Characterization and ontogenesis of nitric oxide synthase activity in pig enterocytes
Author(s) -
M'Rabet-Touil Hamida,
Blachier François,
Morel Marie-Thérèse,
Darcy-Vrillon Béatrice,
Duée Pierre-Henri
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80345-u
Subject(s) - nitric oxide synthase , nitric oxide , arginine , enzyme , cytosol , biochemistry , egta , enzyme assay , biology , chemistry , endocrinology , calcium , amino acid , organic chemistry
Nitric oxide has been implicated as a local modulator of several gastrointestinal functions. In this study, we have measured nitric oxide synthase activity in homogenates of enterocytes isolated from post‐weaned pigs. The enzyme required the presence of NADPH and 6‐(R,S)‐5,6,7,8‐tetrahydro‐ l ‐biopterin. Conversely exogenous FAD and FMN did not appear to be necessary for enzyme activity. The enzyme activity was not affected by added Ca 2+ or EGTA and was inhibited by the arginine analogs N G ‐monomethyl‐ l ‐arginine and N ω ‐nitro‐ l ‐arginine. NO synthase activity was not detectable in enterocytes isolated at birth and increased slightly in suckling animals. NO synthase activity was found to be present mostly in the cytosolic fraction isolated from post‐weaned pigs enterocytes.