Faculty Opinions recommendation of The N-Glycosylation of Mouse Immunoglobulin G (IgG)-Fragment Crystallizable Differs Between IgG Subclasses and Strains.

Author(s):  
Mattias Collin
2017 ◽  
Vol 8 ◽  
Author(s):  
Noortje de Haan ◽  
Karli R. Reiding ◽  
Jasminka Krištić ◽  
Agnes L. Hipgrave Ederveen ◽  
Gordan Lauc ◽  
...  

Molecules ◽  
2003 ◽  
Vol 8 (1) ◽  
pp. 86-91 ◽  
Author(s):  
Jiye Cai ◽  
Yao Chen ◽  
Qingcai Xu ◽  
Yong Chen ◽  
Tao Zhao ◽  
...  

Biochemistry ◽  
1990 ◽  
Vol 29 (24) ◽  
pp. 5727-5733 ◽  
Author(s):  
Takako Igarashi ◽  
Mamoru Sato ◽  
Yukiteru Katsube ◽  
Koji Takio ◽  
Toshiyuki Tanaka ◽  
...  

1968 ◽  
Vol 107 (6) ◽  
pp. 823-828 ◽  
Author(s):  
Alan R. Williamson ◽  
Brigitte A. Askonas

The relative lability of the interchain disulphide bonds of mouse G2a-myeloma protein 5563 was studied as a function of 2-mercaptoethanol concentration. Analysis of partial-reduction mixtures by polyacrylamide-gel electrophoresis and microdensitometry showed that the disulphide bonds between light and heavy chains are much more susceptible to reduction than the bonds between heavy chains. At a low concentration of 2-mercaptoethanol (10mm) the major dissociable products of mouse immunoglobulin G are heavy-chain dimers and free light chains. These findings contrast with the reported behaviour of rabbit immunoglobulin G, for which the lability of inter-heavy-chain bonds was found to exceed that of the bonds linking light and heavy chains (Hong & Nisonoff, 1965); the relative stability of rabbit immunoglobulin G interchain bonds was confirmed in the present study. Examination of human immunoglobulin G and an immunoglobulin G (γ2) of guinea pig showed that at least in the majority of molecules, as with mouse immunoglobulin G, the disulphide bonds between light and heavy chains are more susceptible to reduction than the inter-heavy-chain bonds.


FEBS Letters ◽  
1993 ◽  
Vol 328 (1-2) ◽  
pp. 49-54 ◽  
Author(s):  
Koichi Kato ◽  
Hiroaki Gouda ◽  
Wakana Takaha ◽  
Atsuko Yoshino ◽  
Chigusa Matsunaga ◽  
...  

1987 ◽  
Vol 33 (6) ◽  
pp. 840-844 ◽  
Author(s):  
M H Zweig ◽  
G Csako ◽  
C C Benson ◽  
B D Weintraub ◽  
B B Kahn

Abstract "Sandwich"-type assays are subject to positive interference by the patient's "heterophile" antibodies. If present, these bind to the animal immunoglobulins in the assay reagents, forming artefactual sandwiches indistinguishable from those formed with the analyte itself. Immunoglobulins from non-immunized animals, added to the assay reagents, can diminish this effect by blocking the patient's antibodies. Elsewhere, we studied several patients with anti-mouse immunoglobulin activity, whose serum gave spuriously high results for thyrotropin (TSH) concentrations. Here we have studied this phenomenon by adding, to pooled zero-TSH serum, antibodies to mouse, goat, and horse immunoglobulins and then assaying TSH by several other sandwich-type assays involving mouse monoclonal antibodies. Assays not supplemented with blocking immunoglobulins from mice or other animals were more susceptible to this effect. When large amounts of antibody were added, the antibody excess diminished the interference. However, the presence of blocking immunoglobulins could reverse such antibody excess, actually enhancing, instead of diminishing, the positive interference. Users should be aware that blocking immunoglobulins may diminish but not necessarily eliminate this problem with such assays.


1987 ◽  
Vol 257 (2) ◽  
pp. 387-394 ◽  
Author(s):  
Tsuguo Mizuochi ◽  
Jiharu Hamako ◽  
Koiti Titani

Plant Science ◽  
1999 ◽  
Vol 140 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Pramod Tandon ◽  
Masaya Ishikawa ◽  
Atsushi Komamine ◽  
Hiroo Fukuda

2004 ◽  
Vol 11 (6) ◽  
pp. 1192-1193 ◽  
Author(s):  
G. R. McLean ◽  
K. K. Miller ◽  
J. W. Schrader ◽  
A. K. Junker

ABSTRACT Hyper-immunoglobulin M (IgM) syndrome (HIGM) is a rare heterogeneous primary immune deficiency. We describe a patient with HIGM characterized by skewed production of serum IgG subclasses and normal somatic hypermutation. This case may represent a subgroup of HIGM type 4 that is characterized by a biased switching to the V-region proximal constant regions.


Sign in / Sign up

Export Citation Format

Share Document