Title : Preferential recognition of undisruptable dimers of inducible nitric oxide synthase by a monoclonal antibody directed against an N-terminal epitope.

Pub. Date : 2005 Feb 15

PMID : 15699167






2 Functional Relationships(s)
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1 We have recently shown that intracellular iNOS forms dimers that are "undisruptable (UD)" by heat, SDS, strong denaturants, and/or reducing agents. Sodium Dodecyl Sulfate nitric oxide synthase 2 Homo sapiens
2 Our data suggest that UD-dimers of iNOS, in spite of SDS-PAGE denaturation, still maintain features of the quaternary structure of iNOS particularly at its N-terminal end and including head-to-head contact of the oxygenase domains. Sodium Dodecyl Sulfate nitric oxide synthase 2 Homo sapiens