scholarly journals A λ Bence-Jones protein in guinea pigs

1975 ◽  
Vol 151 (3) ◽  
pp. 751-753 ◽  
Author(s):  
F K Stevenson ◽  
L E Mole ◽  
C M Raymont ◽  
G T Stevenson

1. The L2C lymphocytic leukaemia in strain-2 guinea pigs is accompanied by a protein in the urine resembling a homogenous immunoglobulin light chain. 2. The amino acid sequence over the first 20 residues demonstrates a close analogy with a human λ chain of V region subgroup IV. 3. The protein is apparently synthesized by the leukaemic cells and thus represents a monoclonal light chain, i.e. a Bence-Jones protein.

1997 ◽  
Vol 45 (5) ◽  
pp. 551-556 ◽  
Author(s):  
L. A. OMTVEDT ◽  
G. HUSBY ◽  
G. G. CORNWELL III ◽  
R. A. KYLE ◽  
K. SLETTEN

1990 ◽  
Vol 171 (6) ◽  
pp. 1919-1930 ◽  
Author(s):  
A Puccetti ◽  
T Koizumi ◽  
P Migliorini ◽  
J André-Schwartz ◽  
K J Barrett ◽  
...  

Autoantibodies against the 70-kD U1 RNP nucleoprotein autoantigen and DNA were elicited in normal BALB/c mice with a purified Ig light chain. This light chain, derived from a lupus-prone MRL-lpr/lpr mouse, has two distinctive properties: it contains an idiotypic marker recognized by a monoclonal MRL-lpr/lpr anti-snRNP autoantibody, and the amino acid sequence of its third hypervariable region (CDR3) is homologous to a sequence in an antigenic region of the 70-kD U1 RNP polypeptide. The results demonstrate that an Ig idiotype that mimics an autoantigen can induce autoimmunization.


1974 ◽  
Vol 141 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Jean-Claude Jaton

The amino acid sequence of the N-terminal 139 residues of the L (light) chain derived from a homogeneous rabbit antibody (designated BS-1) to type III pneumococci was determined. A combination of methods involving tryptic cleavage restricted to the 2 arginine residues of the molecule and mild acid hydrolysis of a labile peptide bond between the V (variable) and C (constant) regions of the L chain (Fraser et al., 1972) allowed the isolation of two large peptides comprising the entire V region (residues 1–109); these peptides were suitable for automated Edman degradation. The complete sequence analysis of the V region was carried out with only 4μmol of L chain. This material was homogeneous, although minor variant sequences, if present at the 10% value, would not have been detected. The L chain contains 3 intrachain disulphide bridges, whose pairing was established by diagonal electrophoresis: there is one V-region bridge between positions 23 and 88 and one C-region bridge between positions 134 and 194; the third one connects V and C domains between positions 80 and 171. When compared with the basic sequence of human κ chains, rabbit L chain BS-1 appears to be more similar to the VKI prototype sequence than to VKII or VKIII sequences, where VKI, VKII and VKIII represent subgroups I, II and III respectively of V regions of κ light chains. The V regions of rabbit heavy and light chains are homologous to each other. The presence of two clusters of 3 glycine residues in positions 94–96 and 99–101 respectively is remarkable. Residues 94–96 may be related to antibody complementarity whereas residues 99–101 function probably as a pivot permitting the combining region of the L chain to make optimal contact with the antigenic determinant (Wu & Kabat, 1970).


Author(s):  
Vittorio Bellotti ◽  
Monica Stoppini ◽  
Giampaolo Merlini ◽  
Maria Carla Zapponi ◽  
Maria Laura Meloni ◽  
...  

Biochemistry ◽  
1983 ◽  
Vol 22 (4) ◽  
pp. 993-998 ◽  
Author(s):  
Hammadi Ayadi ◽  
Sophie Dutka ◽  
Pierre Paroutaud ◽  
A. Donny Strosberg

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