Co-reactivity between related and unrelated environmental allergens in equine allergen-specific IgE serology testing in the UK.

Background: Identification of environmental allergens in horses with allergic disease facilitates allergen avoidance and targeted immunotherapy.

Hypothesis/objectives: To evaluate allergenic co-reactivity between 44 environmental allergens.

Animals: Horses with suspected allergic disease (n = 344) whose sera were submitted for environmental allergen testing.

Nanoscale probing reveals that reduced stiffness of clots from fibrinogen lacking 42 N-terminal Bbeta-chain residues is due to the formation of abnormal oligomers.

Removal of Bbetal-42 from fibrinogen by Crotalus atrox venom results in a molecule lacking fibrinopeptide B and part of a thrombin binding site. We investigated the mechanism of polymerization of desBbeta1-42 fibrin. Fibrinogen trinodular structure was clearly observed using high resolution noncontact atomic force microscopy.

Common variation in the C-terminal region of the fibrinogen beta-chain: effects on fibrin structure, fibrinolysis and clot rigidity.

Fibrinogen BbetaArg448Lys is a common polymorphism, positioned within the carboxyl terminus of the Bbeta-chain of the molecule. Studies suggest that it is associated with severity of coronary artery disease and development of stroke. The effects of the amino acid substitution on clot structure remains controversial, and the aim of this study was to investigate the effect(s) of this polymorphism on fibrin clot structure using recombinant techniques.