The Primary Structure of Rabbit and Mouse Immunoglobulin Light Chains: Structural Correlates of Allotypy

1973 ◽  
pp. 51-77 ◽  
Author(s):  
Ettore Appella ◽  
John K. Inman
Keyword(s):  
Primary Structure ◽  
Light Chains ◽  
Immunoglobulin Light Chains ◽  
Mouse Immunoglobulin

Translation of messenger RNA for mouse immunoglobulin light chains in living frog oocytes

1973 ◽  
Vol 80 (3) ◽  
pp. 553-557 ◽  
Author(s):  
M. Smith ◽  
J. Stavnezer ◽  
R.C. Huang ◽  
J.B. Gurdon ◽  
C.D. Lane
Keyword(s):  
Messenger Rna ◽  
Light Chains ◽  
Immunoglobulin Light Chains ◽  
Mouse Immunoglobulin

scholarly journals Heterogeneity in Primary Structure, Post-Translational Modifications, and Germline Gene Usage of Nine Full-Length Amyloidogenic κ1 Immunoglobulin Light Chains†

Biochemistry ◽  
2007 ◽  
Vol 46 (49) ◽  
pp. 14259-14271 ◽  
Author(s):  
Lawreen H. Connors ◽  
Yan Jiang ◽  
Marianna Budnik ◽  
Roger Théberge ◽  
Tatiana Prokaeva ◽  
...  
Keyword(s):  
Primary Structure ◽  
Full Length ◽  
Light Chains ◽  
Germline Gene ◽  
Immunoglobulin Light Chains ◽  
Post Translational Modifications ◽  
Gene Usage

scholarly journals Genetic polymorphism of mouse immunoglobulin light chains revealed by isoelectric focusing.

1976 ◽  
Vol 144 (1) ◽  
pp. 298-303 ◽  
Author(s):  
D Gibson
Keyword(s):  
Isoelectric Focusing ◽  
Inbred Mouse ◽  
Rapid Analysis ◽  
Light Chains ◽  
Mouse Strains ◽  
Immunoglobulin Light Chains ◽  
F1 Hybrid ◽  
Mouse Immunoglobulin ◽  
Gel Isoelectric Focusing ◽  
Hybrid Mice

Light chains isolated from normal immunoglobulin of unimmunized mice were analyzed by gel isoelectric focusing. Examination of the focusing patterns of light chains from nine inbred mouse strains showed that six of the strains (SWR/J, C3H/HeJ, DBA/1J, A/J, CBA/J, and C57BL/6J) possessed a virtually identical spectrum of focusing bands, while the remaining three strains (RF/J, AKR/J, and C58/J) showed clear differences involving several bands. Analysis of the light chains of individual SWR/J, C58/J, and F1 hybrid mice indicated that the differences in focusing pattern were inherited in a simple codominant fashion. A new procedure was developed for the rapid analysis of light chains from small quantities of serum.

scholarly journals GENETIC CORRELATION OF A MOUSE LIGHT CHAIN VARIABLE REGION MARKER WITH A THYMOCYTE SURFACE ANTIGEN

1974 ◽  
Vol 140 (5) ◽  
pp. 1432-1437 ◽  
Author(s):  
Paul D. Gottlieb
Keyword(s):  
Linkage Group ◽  
Surface Antigen ◽  
Strain Distribution ◽  
Congenic Strain ◽  
Variable Region ◽  
Light Chains ◽  
Immunoglobulin Light Chains ◽  
Mouse Immunoglobulin ◽  
Peptide Expression ◽  
Peptide Marker

The inbred and congenic strain distribution of the IH-peptide marker in the variable region of mouse immunoglobulin light chains has been compared with other known genetic markers. A positive correlation was noted between the IH-peptide marker and expression of the Ly-3.1 thymocyte cell surface antigen. This suggests that the locus responsible for IH-peptide expression is genetically linked to the Ly-2 and Ly-3 loci in linkage group XI on chromsome 6 of the mouse.

scholarly journals The Role of Protein Thermodynamics and Primary Structure in Fibrillogenesis of Variable Domains from Immunoglobulin Light Chains

2019 ◽  
Vol 141 (34) ◽  
pp. 13562-13571 ◽  
Author(s):  
Enrico Rennella ◽  
Gareth J. Morgan ◽  
Nicholas Yan ◽  
Jeffery W. Kelly ◽  
Lewis E. Kay
Keyword(s):  
Primary Structure ◽  
Light Chains ◽  
Immunoglobulin Light Chains ◽  
Protein Thermodynamics ◽  
Variable Domains

scholarly journals Human rheumatoid factor crossidiotypes. I. WA and BLA are heat-labile conformational antigens requiring both heavy and light chains.

1986 ◽  
Vol 164 (5) ◽  
pp. 1809-1814 ◽  
Author(s):  
V Agnello ◽  
J L Barnes
Keyword(s):  
Rheumatoid Factor ◽  
Primary Structure ◽  
Binding Activity ◽  
Light Chains ◽  
Heat Denaturation ◽  
Antigen Binding ◽  
Rheumatoid Factors ◽  
Simple Method ◽  
Heat Labile

Evidence was obtained that both the WA and BLA crossidiotype (XId) groups are conformational antigens requiring both L and H chains and that with heat denaturation the antigens that define the XIds and antigen-binding activity are lost in parallel. In contrast, the primary structure-dependent crossreactive idiotype (CRI), PSL2, which is only weakly detected on native Wa and Bla monoclonal rheumatoid factors (mRFs), became prominently detected on the heated Wa and Bla mRFs. Heat denaturation may provide a simple method for distinguishing Ids determined by conformational antigen from primary structure-dependent Ids. In addition to heat denaturation, some acid conditions commonly used for preparation of RFs were also found to cause marked loss of Id antigen. The finding of PSL2-CRI on Bla mRF indicates that this Id is not unique to the WA XId.

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