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Вид документа : Статья из журнала

РЖ ВИНИТИ 34 (BI39) 97.02-04К1.364

Автор(ы) : Fuchs, Hendrik, Orberger, Georg, Tauber, Rudolf, GeSSner, Reinhard
Заглавие : Direct calibration ELISA: A rapid method for the simplified determination of association constants of unlabeled biological molecules
Источник статьи : J. Immunol. Meth. - 1995. - Vol. 188, N 2. - С. 197-208
Аннотация: Were presented a novel method for the rapid determination of association constants. The method is based on the direct calibration of an enzyme-linked immunosorbent assay (dcELISA). It combines kinetic and equilibrium binding experiments and can be performed on a single microtiter plate. The absorbance data are evaluated by several linearized plots. The dcELISA has been used to analyze the binding of a monoclonal antibody, OKT9, to its cognate antigen, the human transferrin receptor, and yielded an association constant of K[a]=2.2*10{9} 1/mol and a complex formation rate constant of k[c]=2.7*10{-4} s{-1}. A 26% larger association constant was obtained with a radioimmunoassay (RIA)-based Scatchard analysis using {125}I-labeled OKT9. By quantifying the binding of the same iodinated antibody with the dcELISA were verified that the iodination modifies the binding properties of the antibody. The dcELISA thus appears to be superior to all methods requiring covalent modifications. In principle, the direct calibration method can also be combined with all other solid phase assays. It should thus expand their scope in quantifying the binding properties of biologically important molecules. Германия, Inst. Klin. Chemie und Biochemie, Humbold-Univ. Berlin. Библ. 21
ГРНТИ : 34.43.17
Предметные рубрики: МОНОКЛОНАЛЬНОЕ АНТИТЕЛО OKT9
СВЯЗЫВАНИЕ С АНТИГЕНОМ
ОПРЕДЕЛЕНИЕ КОНСТАНТЫ СВЯЗЫВАНИЯ
ОПИСАНИЕ МЕТОДА
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Вид документа : Статья из журнала

РЖ ВИНИТИ 34 (BI39) 96.10-04К1.58

Автор(ы) : Mammen, Mathai, Gomez Frank A., Whitesides George M.
Заглавие : Determination of the binding of ligands containing the N-2,4-dinitrophenyl group to bivalent monoclonal rat anti-DNP antibody using affinity capillary electrophoresis
Источник статьи : Anal. Chem. - 1995. - Vol. 67, N 19. - С. 3526-3535
Аннотация: Affinity capillary electrophoresis has been used to determine the two dissociation constants of the complex between anti-DNP rat monoclonal IgG[2b] antibody and charged ligands that contained a N-dinitrophenyl group. Singly and multiply charged ligands were used to establish the influence of the charge on the mobility of the complex between Ig and its ligand(s). For this antibody and these monovalent ligands, the dissociation of the ligands from the antibody occurred noncooperatively. The charge on IgG[2b] at pH 8.3 is estimated to be -8.0; this value is obtained by analysis of the electrophoretic mobilities of complexes IgG[2b]L[2], where the ligands L are structurally similar but have different charges. США, Dep. Chem., Harvard Univ, Cambridge, MA 02138. Библ. 53
ГРНТИ : 34.43.33
Предметные рубрики: АНТИТЕЛА
СВЯЗЫВАЮЩИЕ ЛИГАНДЫ
N-2,4 ДИНИТРОФЕНИЛ
ОПРЕДЕЛЕНИЕ КОНСТАНТЫ СВЯЗЫВАНИЯ
ЗАРЯД АНТИГЕНА
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