Article
The origins of enhanced activity in factor VIIa analogs and the interplay between key allosteric sites revealed by hydrogen exchange mass spectrometry.
The Journal of biological chemistry - 9 May 2008
Rand Kasper D, Andersen Mette D, Olsen Ole H, Jørgensen Thomas J D, Ostergaard Henrik, Jensen Ole N, Stennicke Henning R, Persson Egon
Abstract excerpt
Factor VIIa (FVIIa) circulates in the blood in a zymogen-like state. Only upon association with membrane-bound tissue factor (TF) at the site of vascular injury does FVIIa become active and able to initiate blood coagulation. Here we used hydrogen exchange monitored by mass spectrometry to investigate the conformational effects of site-directed mutagenesis at key positions in FVIIa and the origins of enhanced...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.