scholarly journals Immunoglobulin G heavy chain (Gm) allotypes in multiple sclerosis.

1981 ◽  
Vol 67 (6) ◽  
pp. 1797-1800 ◽  
Author(s):  
J P Pandey ◽  
J M Goust ◽  
J P Salier ◽  
H H Fudenberg
Keyword(s):  
Multiple Sclerosis ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Gm Allotypes

The Immunoglobulin G Heavy Chain Repertoire in Multiple Sclerosis Plaques Is Distinct from the Heavy Chain Repertoire in Peripheral Blood Lymphocytes

2001 ◽  
Vol 98 (2) ◽  
pp. 258-263 ◽  
Author(s):  
Gregory P. Owens ◽  
Mark.P. Burgoon ◽  
Jacqueline Anthony ◽  
Bette K. Kleinschmidt-DeMasters ◽  
Donald H. Gilden
Keyword(s):  
Multiple Sclerosis ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Peripheral Blood ◽  
Peripheral Blood Lymphocytes ◽  
Blood Lymphocytes

IgG Heavy-Chain (GM) Allotypes and Immune Response to Insulin in Insulin-Requiring Diabetes Mellitus

1981 ◽  
Vol 304 (7) ◽  
pp. 407-409 ◽  
Author(s):  
Yoshinobu Nakao ◽  
Hideo Matsumoto ◽  
Tokiko Miyazaki ◽  
Nobuhiko Mizuno ◽  
Naomichi Arima ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Immune Response ◽  
Heavy Chain ◽  
Gm Allotypes

scholarly journals Cerebrospinal-fluid-derived Immunoglobulin G of Different Multiple Sclerosis Patients Shares Mutated Sequences in Complementarity Determining Regions

2013 ◽  
Vol 12 (12) ◽  
pp. 3924-3934 ◽  
Author(s):  
Vaibhav Singh ◽  
Marcel P. Stoop ◽  
Christoph Stingl ◽  
Ronald L. Luitwieler ◽  
Lennard J. Dekker ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Cerebrospinal Fluid ◽  
Immunoglobulin G ◽  
Complementarity Determining Regions ◽  
Multiple Sclerosis Patients

High performance of cerebrospinal fluid immunoglobulin G analysis for diagnosis of multiple sclerosis

2019 ◽  
Vol 266 (4) ◽  
pp. 902-909
Author(s):  
Simon Gamraoui ◽  
Guillaume Mathey ◽  
Marc Debouverie ◽  
Catherine Malaplate ◽  
René Anxionnat ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Cerebrospinal Fluid ◽  
Immunoglobulin G ◽  
High Performance

The cerebrospinal fluid immunoglobulin G index as a diagnostic aid in multiple sclerosis: a Bayesian approach.

1982 ◽  
Vol 28 (2) ◽  
pp. 354-355 ◽  
Author(s):  
E A Hische ◽  
H J van der Helm ◽  
H K van Walbeek
Keyword(s):  
Multiple Sclerosis ◽  
Cerebrospinal Fluid ◽  
Immunoglobulin G ◽  
Graphical Representation ◽  
Likelihood Ratios ◽  
Serum Samples ◽  
Predictive Values ◽  
Definite Multiple Sclerosis ◽  
Igg Index ◽  
Diagnostic Usefulness

Abstract Having determined immunoglobulin G (IgG) and albumin concentrations in 1100 cerebrospinal fluid and serum samples, we calculated the IgG index. Likelihood ratios for multiple sclerosis were calculated by using a training set consisting of 100 patients with definite multiple sclerosis and one consisting of 97 patients suffering from diseases from which multiple sclerosis must be differentiated. Predictive values for multiple sclerosis, given different values for the IgG index, are given in a graphical representation of Bayes' theorem. We conclude that this approach increases the diagnostic usefulness of the IgG index for the diagnosis of multiple sclerosis.

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.

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