Interaction of epitope-related and -unrelated peptides with anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab fragment.
about
Thermodynamic analysis of the binding of 2F5 (Fab and immunoglobulin G forms) to its gp41 epitope reveals a strong influence of the immunoglobulin Fc region on affinity.Isothermal titration calorimetry reveals differential binding thermodynamics of variable region-identical antibodies differing in constant region for a univalent ligand.
P2860
Interaction of epitope-related and -unrelated peptides with anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab fragment.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Interaction of epitope-related ...... dy CB4-1 and its Fab fragment.
@ast
Interaction of epitope-related ...... dy CB4-1 and its Fab fragment.
@en
type
label
Interaction of epitope-related ...... dy CB4-1 and its Fab fragment.
@ast
Interaction of epitope-related ...... dy CB4-1 and its Fab fragment.
@en
prefLabel
Interaction of epitope-related ...... dy CB4-1 and its Fab fragment.
@ast
Interaction of epitope-related ...... dy CB4-1 and its Fab fragment.
@en
P2093
P2860
P356
P1476
Interaction of epitope-related ...... dy CB4-1 and its Fab fragment.
@en
P2093
Heinz Welfle
Karin Welfle
Rolf Misselwitz
Wolfgang Höhne
P2860
P356
10.1002/JMR.607
P577
2003-01-01T00:00:00Z