作者
Masaki Nakane, Jane Mitchell, Ulrich Förstermann, Ferid Murad
发表日期
1991/11/14
期刊
Biochemical and biophysical research communications
卷号
180
期号
3
页码范围
1396-1402
出版商
Academic Press
简介
Nitric oxide synthase purified from rat brain, which is Ca2+ and calmodulin dependent, was phosphorylated by calcium calmodulin-dependent protein kinase II as well as protein kinase C. Phosphorylation by calcium calmodulin-dependent protein kinase II resulted in a marked decrease in enzyme activity (33% of control) without changing the co-factor requirements, whereas a moderate increase in enzyme activity (140% of control) was observed after phosphorylation by protein kinase C. These findings indicate that brain nitric oxide synthase activity may be regulated not only by Ca2+/calmodulin and several co-factors, but also by phosphorylation.
引用总数
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