[24] Induction of rabbit immunoglobulin G antibodies against synthetic sialylated neoglycoproteins

1994 ◽  
pp. 351-361 ◽  
Author(s):  
René Roy ◽  
Craig A. Laferrière ◽  
Robert A. Pon ◽  
Andrzej Gamian
Keyword(s):  
Immunoglobulin G ◽  
Rabbit Immunoglobulin

scholarly journals Anti-rabbit immunoglobulin G detection in complex medium by PM-RAIRS and QCM

2007 ◽  
Vol 22 (12) ◽  
pp. 2884-2890 ◽  
Author(s):  
Elisabeth Briand ◽  
Michèle Salmain ◽  
Chantal Compère ◽  
Claire-Marie Pradier
Keyword(s):  
Immunoglobulin G ◽  
Complex Medium ◽  
Rabbit Immunoglobulin

scholarly journals Differential reduction of interchain disulphide bonds of mouse immunoglobulin G

1968 ◽  
Vol 107 (6) ◽  
pp. 823-828 ◽  
Author(s):  
Alan R. Williamson ◽  
Brigitte A. Askonas
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Polyacrylamide Gel Electrophoresis ◽  
Partial Reduction ◽  
Free Light Chains ◽  
Myeloma Protein ◽  
Heavy Chains ◽  
Disulphide Bonds ◽  
Rabbit Immunoglobulin ◽  
Mouse Immunoglobulin

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.

scholarly journals The disulphide bonds of the heavy chain of rabbit immunoglobulin G

1970 ◽  
Vol 116 (2) ◽  
pp. 261-268 ◽  
Author(s):  
I. J. O'Donnell ◽  
B. Frangione ◽  
R. R. Porter
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Good Yield ◽  
Sequence Variants ◽  
Lower Yield ◽  
Disulphide Bonds ◽  
Rabbit Immunoglobulin ◽  
Minor Sequence

Six peptides containing eight half-cystine residues were isolated in good yield, after either oxidation or reduction and carboxymethylation of fragment C-1, which contains the N-terminal half of the heavy chain of rabbit immunoglobulin G. The sequences of five of these peptides had been reported previously (Cebra, Steiner & Porter, 1968b; Wilkinson, 1969) and that of the sixth was established. Other peptides containing half-cystine residues were isolated in much lower yield and are presumed to be derived from minor sequence variants. The cystine-containing peptides from enzymic digests of whole immunoglobulin G and Fc fraction were studied by several techniques and the results obtained enable us to put forward a scheme of the arrangement of the inter- and intra-chain disulphide bonds.

Proximity relationships within the Fc segment of rabbit immunoglobulin G analyzed by resonance energy transfer

Biochemistry ◽  
1981 ◽  
Vol 20 (10) ◽  
pp. 2927-2936 ◽  
Author(s):  
Robert Luedtke ◽  
Charles S. Owen ◽  
Jane M. Vanderkooi ◽  
Fred Karush
Keyword(s):  
Energy Transfer ◽  
Immunoglobulin G ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Rabbit Immunoglobulin

scholarly journals A Thermodynamic Study of Cooperative Structures in Rabbit Immunoglobulin G

1982 ◽  
Vol 126 (3) ◽  
pp. 517-521 ◽  
Author(s):  
Vladimir M. TISCHENKO ◽  
Vladimir P. ZAV'YALOV ◽  
Gyorgy A. MEDGYESI ◽  
Sergei A. POTEKHIN ◽  
Peter L. PRIVALOV
Keyword(s):  
Immunoglobulin G ◽  
Thermodynamic Study ◽  
Rabbit Immunoglobulin
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