The segmental flexibility of the hinge region of immunoglobulin G (IgG) molecules has been
considered to play important roles in the mediation between antigen recognition and effector …

Materials and Methods Materials. Myeloma protein IgGl (x) Ike-N isolated from the plasma of
a patient with multiple myeloma by precipitation with 44%-saturated ammonium sulfate. The …

Satoshi Endo and Yoji Arata* Department of Biophysics and Biochemistry, University of
Tokyo, Hongo, Tokyo 113, Japan Received July 19, 1984 abstract: A high-resolutionnuclear …

CD spectra of the constant region halves of human immunoglobulin G heavy and light
chains have been studied. These studies demonstrate the presence of some β structured …

The hinge region links the antigen binding Fab part to the constant Fc domain in
immunoglobulins. For the hinge peptide derivative [AcThr (OtBu)‐Cys‐Pro‐Pro‐Cys‐Pro …

The circular dichroism spectra, between 210 and 320 nm, of human pooled IgG, two IgG
myeloma proteins and their isolated heavy and light chains have been determined. Below …

On the heat absorption curves of human immunoglobulin G3 (hIgG3) Kuc melting the
scanning calorimetry method reveals a high-temperature (high-Tm) peak of high intensity …

Publisher Summary This chapter summarizes the various studies of the movement of Ig
subunits—that is, segmental flexibility as well as internal motion in the subunits themselves …

Human IgG2 consists of disulfide‐mediated structural isoforms, classified by the number of
Fab arms disulfide‐linked to the heavy chain hinge. In the IgG2‐B isoform, both Fab arms …

The isotropic mobility of separate regions of the intact molecule of immunoglobulin M (IgM)
and its Fab and (Fc) 5 fragments was studied using spin-labeling of carbohydrate (2, 2, 6, 6 …