Structural Studies of Human Immunoglobulin D Myeloma Proteins: Circular-Dichroic Studies of Two Intact Proteins and Enzymically Derived Fragments

1977 ◽  
Vol 5 (1) ◽  
pp. 279-282 ◽  
Author(s):  
ROYSTON JEFFERIS ◽  
JOHN B. MATTHEWS ◽  
PETER BAYLEY
Keyword(s):  
Human Immunoglobulin ◽  
Structural Studies ◽  
Intact Proteins ◽  
Myeloma Proteins ◽  
Immunoglobulin D ◽  
Circular Dichroic

Epitope analysis of human immunoglobulin D with a mouse monoclonal anti-Fab δ chain antibody

2002 ◽  
Vol 319 (1) ◽  
pp. 1-8
Author(s):  
Masaaki Arakawa ◽  
Yoshihisa Itoh ◽  
Naofumi Yoshioka ◽  
Ikunosuke Sakurabayashi
Keyword(s):  
Human Immunoglobulin ◽  
Epitope Analysis ◽  
Immunoglobulin D ◽  
Δ Chain

Human immunoglobulin D segments encoded in tandem multigenic families

Nature ◽  
1981 ◽  
Vol 294 (5842) ◽  
pp. 631-635 ◽  
Author(s):  
U. Siebenlist ◽  
J. V. Ravetch ◽  
S. Korsmeyer ◽  
T. Waldmann ◽  
P. Leder
Keyword(s):  
Human Immunoglobulin ◽  
Immunoglobulin D

Isolation of Murine and Human Immunoglobulin M and Murine Immunoglobulin D

2009 ◽  
Vol 85 (1) ◽  
Author(s):  
Sarah M. Andrew ◽  
Julie A. Titus ◽  
Ashok Amin ◽  
Richard Coico
Keyword(s):  
Immunoglobulin M ◽  
Human Immunoglobulin ◽  
Immunoglobulin D

scholarly journals STRUCTURAL STUDIES OF HUMAN IMMUNOGLOBULINS

1965 ◽  
Vol 122 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Blas Frangione ◽  
Edward C. Franklin
Keyword(s):  
Antigenic Specificity ◽  
Structural Studies ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Myeloma Proteins ◽  
Peptide Maps

1. Comparison of peptide maps of the Fc fragments of normal G immunoglobulins and 11 G myeloma proteins of the We (b) type showed them to be very similar except for differences associated with the Gm type. Some additional differences were noted, however, in the Fc fragments of three Vi (c) myeloma proteins. 2. Peptide maps of heavy chains from the same G myeloma proteins differed from each other and from normal heavy chains. In general, the myeloma chains contained a larger number of well defined spots; some of these were common to normal heavy chains while others were unique to each protein. Others, present in normal heavy chains, were lacking in the myeloma proteins. 3. Comparison of the heavy chains and Fc fragments from the same protein suggests that much of the variability of different myeloma proteins and, presumably, antibodies resides in the Fd fragment. 4. Further support for this is given by the finding that the antigenic specificity of 3 myeloma proteins also appeared to reside in the Fd fragments.

scholarly journals Streptococcus pyogenes type M12 protein shows selective binding to some human immunoglobulin G3 myeloma proteins.

1994 ◽  
Vol 62 (8) ◽  
pp. 3559-3563 ◽  
Author(s):  
P J Johansson ◽  
C C Malone ◽  
R C Williams ◽  
D S Retnoningrum ◽  
P P Cleary
Keyword(s):  
Streptococcus Pyogenes ◽  
Human Immunoglobulin ◽  
Selective Binding ◽  
Myeloma Proteins
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