PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 3391651

Functional and structural implications of variable region immunoglobulin dynamic states.

E W Voss·M A Dombrink-Kurtzman·S D Miklasz
View original source ↗Export metadata ↓

Abstract

The consequence of multiple conformational states in the immunoglobulin variable region are considered. Bound ligand is viewed as a stabilizer of one conformer from a series of non-liganded conformers. Kinetic, equilibrium, thermodynamic and crystal formation information are used as supporting evidence for a unique conformer which is the crystallizable liganded state. The multi-state model is discussed in terms of certain biological and biochemical properties exhibited by the immunoglobulin molecule.

Explore related subjects

Antigen-Antibody ReactionsBinding Sites, AntibodyImmunoglobulin Fab FragmentsImmunoglobulin Variable RegionKineticsMotionProtein ConformationJournal ArticleResearch Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

E W Voss, M A Dombrink-Kurtzman, S D Miklasz. 1988. Functional and structural implications of variable region immunoglobulin dynamic states.. https://doi.org/10.3109/08820138809055716

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↗