Mouse immunoglobulin genes: a bacterial plasmid containing the entire coding sequence for a pre-γ 2a heavy chain

We have begun to purify and characterize several proteins which bind to the mouse immunoglobulin heavy-chain enhancer to understand the molecular interactions important for enhancer activity. Three proteins which bind to different sites on the immunoglobulin heavy-chain enhancer have been chromatographically separated and partially purified. One protein binds a site which has not been reported previously and does not bind to other reported protein-binding sites on the immunoglobulin heavy-chain enhancer. Binding-site boundaries for the three partially purified proteins have been precisely mapped by methylation interference, DNase I footprinting, and orthophenanthroline/copper chemical nuclease footprinting. We have also characterized these three proteins with respect to dissociation rate constants.

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Nuclear transcripts of mouse heavy chain immunoglobulin genes contain only the expressed class of C-region sequences

Science ◽

10.1126/science.109919 ◽

1979 ◽

Vol 204 (4397) ◽

pp. 1087-1088 ◽

Cited By ~ 16

Author(s):

K. Marcu ◽

U Schibler ◽

R. Perry

Keyword(s):

Heavy Chain ◽

Immunoglobulin Genes

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Expression of mouse immunoglobulin light and heavy chain variable regions in Escherichia coli and reconstitution of antigen-binding activity

Protein Engineering Design and Selection ◽

10.1093/protein/3.7.641 ◽

1990 ◽

Vol 3 (7) ◽

pp. 641-647 ◽

Cited By ~ 31

Author(s):

Helen Field ◽

G.T. Yarranton ◽

A.R. Rees

Keyword(s):

Escherichia Coli ◽

Heavy Chain ◽

Binding Activity ◽

Antigen Binding ◽

Variable Regions ◽

Mouse Immunoglobulin

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Molecular cloning of mouse immunoglobulin heavy chain messenger ribonucleic acids coding for .mu., .alpha., .gamma.1, .gamma.2a, and .gamma.3 chains

Biochemistry ◽

10.1021/bi00553a027 ◽

1980 ◽

Vol 19 (12) ◽

pp. 2711-2719 ◽

Cited By ~ 16

Author(s):

Jerry M. Adams ◽

Nicholas M. Gough ◽

Elizabeth A. Webb ◽

Brett M. Tyler ◽

Jillian Jackson ◽

...

Keyword(s):

Molecular Cloning ◽

Heavy Chain ◽

Immunoglobulin Heavy Chain ◽

Ribonucleic Acids ◽

Mouse Immunoglobulin

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Developmental Aspects of Mucosal Immunoglobulin Genes: Organization and Expression of IgA Heavy-Chain, Polymeric Immunoglobulin Receptor, and J-Chain Genes

Handbook of Mucosal Immunology ◽

10.1016/b978-0-12-524730-6.50014-2 ◽

1994 ◽

pp. 105-111 ◽

Cited By ~ 2

Author(s):

Katherine L. Knight

Keyword(s):

Heavy Chain ◽

Polymeric Immunoglobulin Receptor ◽

Immunoglobulin Genes ◽

Immunoglobulin Receptor ◽

J Chain

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Differential reduction of interchain disulphide bonds of mouse immunoglobulin G

Biochemical Journal ◽

10.1042/bj1070823 ◽

1968 ◽

Vol 107 (6) ◽

pp. 823-828 ◽

Cited By ~ 12

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.

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