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A NO synthase (NOS, EC 1.14.23) was isolated from human cerebellum by two sequential chromatography steps, that is affinity chromatography on 2'5'ADP sepharose and size exclusion chromatography on Superose 6. Human NOS migrated as a single band of 160 kDa on SDS/PAGE. The enzyme was Ca2+/calmodulin-regulated and NADPH/tetrahydrobiopterin (BH4)-dependent, which are characteristics of a type I NOS previously isolated from rat cerebellum. Antisera raised against purified rat cerebellar NOS crossreacted specifically with a 160 kDa protein in crude supernatant fraction of human cerebellum and purified human NOS but not in crude supernatant fraction of the temporal lobe. These findings provide evidence that nitrinergic signal transduction through conversion of L-arginine to L-citrulline and NO does also occur in humans and NO may function as a neurotransmitter in the human central nervous system.
H H Schmidt, and
F Murad
April 2004,
Journal of biochemistry,
H H Schmidt, and
F Murad
February 1994,
The Biochemical journal,
H H Schmidt, and
F Murad
January 1999,
The Journal of biological chemistry,
H H Schmidt, and
F Murad
May 1995,
FEBS letters,
H H Schmidt, and
F Murad
March 1973,
Birth defects original article series,
H H Schmidt, and
F Murad
January 2003,
Advances in experimental medicine and biology,
H H Schmidt, and
F Murad
November 1987,
The Journal of biological chemistry,
H H Schmidt, and
F Murad
April 1975,
Proceedings of the National Academy of Sciences of the United States of America,
H H Schmidt, and
F Murad
May 1987,
Archives of biochemistry and biophysics,
H H Schmidt, and
F Murad
March 1989,
Plant physiology,
