Demonstration of two distinct light chains in HLA-DR-associated antigens by two-dimensional gel electrophoresis

1982 ◽  
Vol 12 (3) ◽  
pp. 214-221 ◽  
Author(s):  
Theonne A. De Kretser ◽  
Michael J. Crumpton ◽  
Julia G. Bodmer ◽  
Walter F. Bodmer
Keyword(s):  
Gel Electrophoresis ◽  
Light Chains ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Hla Dr

scholarly journals Demonstration of structural polymorphism among HLA-DR light chains by two-dimensional gel electrophoresis.

1980 ◽  
Vol 151 (1) ◽  
pp. 144-165 ◽  
Author(s):  
D A Shackelford ◽  
J L Strominger
Keyword(s):  
Cell Lines ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Light Chains ◽  
Two Dimensional ◽  
Structural Polymorphism ◽  
Two Dimensional Gel Electrophoresis ◽  
Hla Dr ◽  
Sds Page

Human HLA-DR antigens were immunoprecipitated from Nonidet P-40 extracts of [35S]methionine-labeled B lymphoblastoid cell lines and compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing (IEF). Two-dimensional (2-D) gel analyses, combining SDS-PAGE in the first dimension and IEF in the second dimension, revealed that the heavy (alpha) and light (beta) chains of each DRw specificity displays microheterogeneity of charge. However, the pattern of the heavy chain did not vary among different DRw specificities. In contrast, the light chains of different DRw types varied both in apparent size and charge distribution. Removal of sialic acids with neuraminidase or inhibition of glycosylation with tunicamycin reduced the microheterogeneity of both DR subunits. However, the heavy and light chains each still focused as two major bands, suggesting that other post-translational modifications contribute to the microheterogeneity or that there are two nonallelic DR-like molecules. After treatment with either neuraminidase or tunicamycin, the DR light chains, but not the heavy chains, were still structurally polymorphic. The DR light chains of serologically cross-reactive specificities displayed similar 2-D gel patterns suggesting that the structural polymorphism of the DR light chains is the basis for the serologically detected polymorphism of the HLA-DR antigens. Two additional polypeptides were observed in immunoprecipitates of DR antigens. These proteins, designated M1 and M2, both had a basic isoelectric point and were invariant among different cell lines. The protein M1 may be intracellular because it can not be immunoprecipitated from the cell surface.

scholarly journals Resolution of Myocardial Myosin Light Chains by Two-Dimensional Gel Electrophoresis

1974 ◽  
Vol 249 (3) ◽  
pp. 994-996
Author(s):  
John McPherson ◽  
Robert R. Traut ◽  
Dean T. Mason ◽  
Robert Zelis ◽  
Joan Wikman-Coffelt
Keyword(s):  
Gel Electrophoresis ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

scholarly journals Demonstration of a third structurally distinct human Ia beta chain by two-dimensional gel electrophoresis.

1982 ◽  
Vol 156 (2) ◽  
pp. 652-657 ◽  
Author(s):  
R W Karr ◽  
C C Kannapell ◽  
J A Stein ◽  
T C Fuller ◽  
R J Duquesnoy ◽  
...  
Keyword(s):  
Cell Lines ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Beta Chain ◽  
Two Dimensional Gel Electrophoresis ◽  
Hla Dr

Previous studies have indicated that HLA-DR homozygous cell lines express two Ia alpha and Ia beta chains that combine to form at least two Ia molecules. This report demonstrates by two-dimensional gel electrophoresis the existence of a third structurally distinct human Ia beta chain on DR2 and DR5 cell lines. This suggests that at least five separate genes control the expression of Ia molecules on HLA-DR homozygous cell lines.

scholarly journals Two-dimensional gel electrophoretic analysis of the MT3 and DR4 molecules from the different D-typed cells.

1984 ◽  
Vol 160 (3) ◽  
pp. 751-758 ◽  
Author(s):  
M Suzuki ◽  
T Yabe ◽  
M Satake ◽  
T Juji ◽  
H Hamaguchi
Keyword(s):  
Light Chain ◽  
Gel Electrophoresis ◽  
Electrophoretic Analysis ◽  
Structural Heterogeneity ◽  
Class Ii ◽  
Light Chains ◽  
Two Dimensional ◽  
Structural Polymorphism ◽  
Two Dimensional Gel Electrophoresis

This report demonstrates directly, using two-dimensional gel electrophoresis and alloantisera, the following: (a) The DR4 light chains show a structural polymorphism among the Dw4, DKT2, and DYT cells. (b) Most of the class II light chains consist of the DR light chain. (c) The MT3 molecule is distinct from the DR4 molecule in the Dw4, DKT2, and DYT cells. (d) The MT3 molecule does not show any structural heterogeneity among the Dw4, DKT2, and DYT cells. These results suggest that the dissection of the D specificity among Dw4, DKT2, and DYT is mainly caused by the differences of the DR4 molecules.

HLA-DR antigens in multiple sclerosis: Two-dimensional gel electrophoresis

Neurology ◽  
1985 ◽  
Vol 35 (2) ◽  
pp. 248-248 ◽  
Author(s):  
S. Sriram ◽  
G. J. Stewart ◽  
M. Buhler ◽  
C. Grumet ◽  
E. Engleman
Keyword(s):  
Multiple Sclerosis ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Hla Dr

Two-dimensional gel electrophoresis of serum specimens from patients with monoclonal gammopathies.

1982 ◽  
Vol 28 (4) ◽  
pp. 900-907 ◽  
Author(s):  
R P Tracy ◽  
R M Currie ◽  
R A Kyle ◽  
D S Young
Keyword(s):  
Gel Electrophoresis ◽  
Light Chains ◽  
Correct Identification ◽  
Two Dimensional ◽  
Excellent Correlation ◽  
Serum Samples ◽  
Two Dimensional Gel Electrophoresis ◽  
Monoclonal Gammopathies ◽  
Heavy Chains ◽  
Electrophoresis System

Abstract We modified the ISO-DALT two-dimensional gel electrophoresis system to allow the routine examination of serum specimens from patients with monoclonal gammopathies. This system, MC-Iso 1, is characterized by a broad pH gradient for resolving the basic immunoglobulin heavy and light chains. The increased resolution of basic proteins may be explained on theoretical grounds by an increase in voltage in this region of the cell. Ancillary techniques, such as those for albumin removal and pI assignment through use of charge standards, have also been implemented. The locations of immunoglobulin heavy chains have been confirmed by examination of over 250 serum samples as well as by "electro-blotting," with use of specific antisera. IgG subclass may also be predicted by location, but not with perfect accuracy. Differentiation of kappa and lambda light chains by relative mobility has been examined; the predictive value for correct identification of kappa chains is 83%, that for lambda chains 69%. Several unknown proteins have been observed in macroglobulinemia, related to mu heavy chain. Finally, we have determined that there is excellent correlation between non-denaturing isoelectric focusing and our system for pI assignment of light chains. This has importance due to reports of the potential importance of light-chain pI in the development of renal disease in patients with monoclonal gammopathies.

Diversity of Glycoprotein Deficiencies in Glanzmann’s Thrombasthenia

1985 ◽  
Vol 54 (03) ◽  
pp. 626-629 ◽  
Author(s):  
M Meyer ◽  
F H Herrmann
Keyword(s):  
High Resolution ◽  
Gel Electrophoresis ◽  
Type Ii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Structural Variant ◽  
Glanzmann’S Thrombasthenia ◽  
Crossed Immunoelectrophoresis ◽  
Glanzmann's Thrombasthenia ◽  
Platelet Proteins

SummaryThe platelet proteins of 9 thrombasthenic patients from 7 families were analysed by high resolution two-dimensional gel electrophoresis (HR-2DE) and crossed immunoelectrophoresis (CIE). In 7 patients both glycoproteins (GPs) IIb and Ilia were absent or reduced to roughly the same extent. In two related patients only a trace of GP Ilb-IIIa complex was detected in CIE, but HR-2DE revealed a glycopeptide in the position of GP Ilia in an amount comparable to type II thrombasthenia. This GP Ilia-like component was neither recognized normally by anti-GP Ilb-IIIa antibodies nor labeled by surface iodination. In unreduced-reduced two-dimensional gel electrophoresis two components were observed in the region of GP Ilia. The assumption of a structural variant of GP Ilia in the two related patients is discussed.

Sign in / Sign up

Export Citation Format

Share Document