PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7859718

Focused antigen capture immunoassay.

K K Suen·W H Lewis
View original source ↗Export metadata ↓

Abstract

A new approach is described to immunoblotting in which antigens after isoelectric focusing are capture on nitrocellulose membranes coated with a specific antibody. The method has been applied to the analysis of human IgA kappa and lambda from whole blood and serum without prior purification. The visualized bands were quantified by laser densitometry in four pI ranges. It is concluded that, under the conditions used, close to 100% of serum IgA is captured. The method has a coefficient of variation of 4.5-12.8%, mean 8.0%.

Explore related subjects

Antigen-Antibody ReactionsAntigensBlood Specimen CollectionHumansHydrogen-Ion ConcentrationImmunoblottingImmunoglobulin AImmunoglobulin kappa-ChainsImmunoglobulin lambda-ChainsIndicators and ReagentsIsoelectric FocusingComparative StudyJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

K K Suen, W H Lewis. Focused antigen capture immunoassay.. https://doi.org/10.1002/elps.11501501169

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Thermodynamic and kinetic analysis of the interaction between hepatitis B surface antibody and antigen on a gold electrode modified with cysteamine and colloidal gold via electrochemistry.

Hepatitis B surface antibody (HBsAb) was immobilized to the surface of a gold electrode modified with cysteamine and colloidal gold as matrices to detect hepatitis B surface antigen (HBsAg). Differential pulse voltammetry (DPV) method was used for the investigation of the specific interaction between the immobilized HBsAb and HBsAg in solution, which was followed as a change of peak current in DPV with time. With the modified gold electrode, the differences in affinity of HBsAb with HBsAg at the temperatures of 37 and 40 degrees C were easily distinguished and the kinetic rate constants (k(ass) and k(diss)) and kinetic affinity constant K were determined from the curves of current versus time. In addition, the thermodynamic constants, DeltaG, DeltaH and DeltaS, of the interaction at 37 degrees C were calculated, which were -56.65, -64.54 and -25.45 kJ mol(-1), respectively.

Antigen-Antibody Reactions↗
PubMed2007

Impact of different inhibitor reactivities with commercial factor VIII concentrates on thrombin generation.

In order to describe the haemostatic role of a variation in inhibitor reactivity with different factor VIII (FVIII) concentrates, we have compared inhibitor titres against a panel of FVIII concentrates and correlated titre with the capacity to inhibit thrombin generation. Three plasma-derived concentrates were tested in vitro in mixing experiments with inhibitor plasmas from 11 patients with severe haemophilia A: Fanhdi, which contains von Willebrand factor (VWF) with a final ratio of approximately 1:1 (VWF IU per IU FVIII:C); Haemate-P with a ratio of 2.5:1 and Hemofil-M containing only trace amounts of VWF. In addition, the recombinant FVIII concentrate Kogenate Bayer containing no VWF was included. Inhibitor titres and the capacity to generate thrombin were measured. A statistically significant difference in measured titres was found with the highest titres recorded against Hemofil-M. The inhibitor titres needed to inhibit 50% maximum thrombin generation were the lowest for Kogenate Bayer and the highest and similar for Fanhdi and Haemate-P with intermediate titres needed for inhibition of Hemofil-M. In this study, the thrombin generation assay provides additional indications for the role of VWF in the treatment of patients with inhibitors. The VWF-containing concentrates Fanhdi and Haemate-P, added to FVIII-deficient plasma with the presence of inhibitor, generate more thrombin than do the purified concentrates Hemofil-M and Kogenate Bayer.

Antigen-Antibody Reactions↗