M
M. P. Esnouf
Researcher at University of Oxford
Publications - 7
Citations - 420
M. P. Esnouf is an academic researcher from University of Oxford. The author has contributed to research in topics: Factor VII & Thrombin. The author has an hindex of 6, co-authored 7 publications receiving 419 citations.
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Journal ArticleDOI
The Isolation and Properties of the Thrombin-like Activity from Ancistrodon rhodostoma Venom
M. P. Esnouf,G. W. Tunnah +1 more
TL;DR: The isolation and characterization of the thrombin-like activity from the whole venom is described, finding that dogs injected with partially purified preparations of the venom would be protected from artificially induced thrombosis of the vena cava.
Journal ArticleDOI
Assay of factor VII activity by two techniques: evidence for increased conversion of VII to αVIIa in hyperlipidaemia, with possible implications for ischaemic heart disease
TL;DR: Factor VII was assayed in healthy adults and pregnant women by a coagulation method (VIIc) and a procedure based upon activation of factor X (VIIt) and the relative values of VIIc and VIIt are proposed as a measure of flux within the coagulated system, and as a measures of coagulability in hyperlipidaemia and other states.
Journal ArticleDOI
An association between the factor VII coagulant activity and thrombin activity induced by surface/cold exposure of normal human plasma
G.J. Miller,M. J. Seghatchian,S. J. Walter,D. J. Howarth,S.G. Thompson,M. P. Esnouf,T W Meade +6 more
TL;DR: The results suggest that VIIC is an index of flux within the coagulation system and support the hypothesis that a high VIIc is an indicator of a hypercoagulable state.
Journal ArticleDOI
The autoactivation of factor XII in the presence of long-chain saturated fatty acids--a comparison with the potency of sulphatides and dextran sulphate.
K.A. Mitropoulos,M. P. Esnouf +1 more
TL;DR: The incubation of purified human factor XII (Hageman factor [HF] in the presence of long-chain saturated fatty acids like stearate or behenate resulted in a time-dependent increase of amidolytic activity, and autoactivation rates followed Michaelis-Menten kinetics.
Journal ArticleDOI
The inhibition of activated Factor X with di: isopropyl fluorophosphate.
J. E. Leveson,M. P. Esnouf +1 more
TL;DR: The amino acid sequence about the site of binding of the di:isopropyl moiety has been shown to be gly.ser‐P‐gly.asp, and the esterase and coagulant activities of activated Factor X have been inhibited by radioactive di:ISOPropyl fluorophosphate.