Use of monoclonal antibodies against rat immunoglobulin light chains in radioimmunoassay of differentiated mouse lymphocyte antigens

1984 ◽  
Vol 98 (3) ◽  
pp. 1228-1231
Author(s):  
A. V. Chervonskii ◽  
A. V. Filatov ◽  
V. V. Cherepakhin ◽  
B. D. Brondz
Keyword(s):  
Monoclonal Antibodies ◽  
Light Chains ◽  
Immunoglobulin Light Chains ◽  
Mouse Lymphocyte ◽  
Lymphocyte Antigens

Production and characterization of monoclonal antibodies specific for the functional domains of poly(ADP-ribose) polymerase

1986 ◽  
Vol 64 (4) ◽  
pp. 368-376 ◽  
Author(s):  
Daniel Lamarre ◽  
Brian Talbot ◽  
Yvan Leduc ◽  
Sylviane Muller ◽  
Guy Poirier
Keyword(s):  
Monoclonal Antibodies ◽  
Dna Binding ◽  
Binding Site ◽  
Limited Proteolysis ◽  
Antigenic Site ◽  
Light Chains ◽  
Immunoglobulin Light Chains ◽  
Substrate Binding Site ◽  
Dna Binding Site

Monoclonal antibodies were developed against poly(ADP-ribose) polymerase and analyzed for their reactivity against the NAD+- and DNA-binding fragments. Two fusions were performed to obtain hybridomas and the resulting anti-poly(ADP-ribose) polymerase antibodies were further screened by characterization of their immunoglobulin light chains. Five different hybridomas were isolated which produced different immunoglobulin light chains, all of which were specific for poly(ADP-ribose) polymerase. The specificities of these antibodies were determined by immunoblotting against the purified poly(ADP-ribose) polymerase, its autodegradation fragments, and the fragments prepared by limited proteolysis with chymotrypsin and papain. These fragments have been suggested to contain the NAD+-binding site, the DNA-binding site, and the automodification site, respectively. All the monoclonal antibodies reacted with the 116 kdalton (kDa) band corresponding to the purified enzyme. Four antibodies reacted exclusively with antigenic site(s) on the 46-kDa fragment which contains the DNA-binding site. A fifth antibody reacted exclusively with a clearly different antigenic site on the 74- and 54-kDa fragments which possess the NAD+ (substrate) binding site. The immunoreactivity with the major autodegradation products (69- and 46-kDa fragments) of the purified enzyme confirms this difference between the two groups of antibodies. The 22-kDa fragment corresponding to the automodification site does not show any immunoreactivity with the antibodies.

Diversity of expressed V and J regions of immunoglobulin light chains in Xenopus laevis

1993 ◽  
Vol 23 (8) ◽  
pp. 1980-1986 ◽  
Author(s):  
Sue E. Stewart ◽  
Louis Du Pasquier ◽  
Lisa A. Steiner
Keyword(s):  
Xenopus Laevis ◽  
Light Chains ◽  
Immunoglobulin Light Chains

Dissociation and fractionation of heavy and light chains from IgG monoclonal antibodies

2011 ◽  
Vol 1218 (17) ◽  
pp. 2402-2404 ◽  
Author(s):  
Pete Gagnon ◽  
George Rodriquez ◽  
Simin Zaidi
Keyword(s):  
Monoclonal Antibodies ◽  
Light Chains
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