Title : Differential response of basal and tetrahydrobiopterin-stimulated activities of placental type III nitric oxide synthase to sodium dodecyl sulphate: relation to dimeric structure.

Pub. Date : 1998 Dec

PMID : 9872368






5 Functional Relationships(s)
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1 SDS (> or =0.05% w/v) resulted in significant inhibition both of basal and BH4-stimulated activities of NOS III, but the latter responded more sensitively. sapropterin nitric oxide synthase 3 Homo sapiens
2 Considering that basal activity is due to the presence of endogenous BH4 tightly bound to the enzyme, this differential sensitivity of basal and BH4-stimulated enzyme activities to SDS may be related to a putative differential protective effect of BH4 on the two subunits of the NOS III dimer. sapropterin nitric oxide synthase 3 Homo sapiens
3 Considering that basal activity is due to the presence of endogenous BH4 tightly bound to the enzyme, this differential sensitivity of basal and BH4-stimulated enzyme activities to SDS may be related to a putative differential protective effect of BH4 on the two subunits of the NOS III dimer. sapropterin nitric oxide synthase 3 Homo sapiens
4 Considering that basal activity is due to the presence of endogenous BH4 tightly bound to the enzyme, this differential sensitivity of basal and BH4-stimulated enzyme activities to SDS may be related to a putative differential protective effect of BH4 on the two subunits of the NOS III dimer. sapropterin nitric oxide synthase 3 Homo sapiens
5 A model describing the interaction between BH4 and NOS III, and its implications on the physiology and pathology of the human placenta, is discussed. sapropterin nitric oxide synthase 3 Homo sapiens