Amino acid sequence of rabbit light chains: variable region of a light chain from a homogeneous immunoglobulin raised by streptococcal immunization

Biochemistry ◽  
1976 ◽  
Vol 15 (7) ◽  
pp. 1381-1386 ◽  
Author(s):  
A. L. Thunberg ◽  
T. J. Kindt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Variable Region ◽  
Light Chains

Antigenische Klassifizierung der Paraproteine und normalen Immunoglobuline vom Lambda-Typ / Paraproteins and Normal Immunoglobulins of the Lambda Type: Immunochemical Differentiation and Classification

1971 ◽  
Vol 26 (12) ◽  
pp. 1292-1302 ◽  
Author(s):  
F. W. Tischendorf
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Variable Region ◽  
Basic Amino Acid ◽  
Light Chains ◽  
Antigenic Sites ◽  
Normal Individuals ◽  
Normal Light ◽  
Bence Jones Proteins

The elaboration of antisera recognizing antigenic sites of the variable region of pathological immunoglobulin λ chains (Bence-Jones-proteins) is described. The antisera react with the (St+) marker carried by Bence-Jones-proteins of the basic amino-acid sequence VλI and the (111+) marker carried by L-chains of the basic sequence VλIII. With these antisera three specificityregion subtypes of human λ immunoglobulin chains could be distinguished antigenically. Twenty randomly chosen normal individuals were shown to be associated with λ chains of both basic sequences, VλI and VλIII. The results provide evidence for the non-allelic nature of the two aminoterminal light chain forms (p<0.001) and suggest that the basic sequences VλI and VλIII of Bence-Jones-proteins represent two distinct subgroups of normal light chains.

scholarly journals A genetic polymorphism in the constant region of rabbit b4 kappa chains.

1976 ◽  
Vol 143 (6) ◽  
pp. 1475-1482 ◽  
Author(s):  
J A Sogn ◽  
T J Kindt
Keyword(s):  
Amino Acid ◽  
Genetic Polymorphism ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Light Chains ◽  
Amino Acid Substitutions ◽  
Constant Region ◽  
Inheritance Pattern ◽  
Amino Acid Sequence Analysis

Amino acid sequence analysis of a b4 light chain from a rabbit homogeneous antistreptococcal antibody revealed the presence of two amino acid substitutions in the constant region not previously reported for these positions. These interchanges, consisting of serine for alanine at position 121 and leucine for glutamine at position 124, were also present in about 30% of the pooled b4 light chains isolated from pooled IgG from the rabbit (4539) that produced the homogeneous antibody. In addition, these interchanges (b4var) were found, always at the same levels, in varying percentages in nonimmune or early immune bleedings from related rabbits in this pedigreed family and could be traced for five generations. The inheritance pattern of b4var was consistent with autosomal codominant inheritance.

scholarly journals The complete amino acid sequence of a prototype immunoglobulin-λ light-chain-type amyloid-fibril protein AR

1981 ◽  
Vol 195 (3) ◽  
pp. 561-572 ◽  
Author(s):  
K Sletten ◽  
J B Natvig ◽  
G Husby ◽  
J Juul
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Amyloid Fibril ◽  
Variable Region ◽  
Amino Acid Residues ◽  
Variable Regions ◽  
Light Chain Type ◽  
Amyloid Fibril Protein ◽  
Chain Type

The amino acid sequence of an amyloid-fibril protein of immunoglobulin light-chain type (AL) was elucidated. The sequence determination involved digesting the protein with trypsin, thermolysin and pepsin. The protein was found to consist of 154 amino acid residues and is thus missing about half of the constant region of a light chain. A certain heterogeneity in the length of the polypeptide was observed in the C-terminal region. The amino acid sequence from CDR (complementary-determining region) 1 and FR (framework region) 3 indicated an oligoclonal origin of the protein. By comparing the primary structure of protein AR with other lambda- and even kappa-chains, it was revealed that protein AR had an insertion of two residues of aspartic acid, namely residues 68 and 69, which has not been reported previously in light chains. The overall sequence homology in the variable region showed that protein AR is more similar to V lambda V than to the other subgroups [Kabat, Wu & Bilofsky (1979) Variable regions of Immunoglobulin Chains, Medical Computer Systems, Bolt, Beranek and Newman, Cambridge, MA].

scholarly journals Amino acid-sequence variability at the N-terminal extra piece of mouse immunoglobulin light-chain precursors of the same and different subgroups

1976 ◽  
Vol 157 (1) ◽  
pp. 145-151 ◽  
Author(s):  
Y Burstein ◽  
I Schechter
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Variable Region ◽  
Amino Acid Residues ◽  
Free System ◽  
Methionine Residue ◽  
N Terminus ◽  
Mouse Myeloma

The proteins programmed in the wheat-germ cell-free system by the mRNA coding for the MOPC-63 mouse myeloma L (light) chain were labelled with six radioactive amino acids: [35S]methionine, [4,5-3H]leucine, [3,4-3H]proline, [3-3H]serine, [4,5-3H]isoleucine or [2,3-3H]alanine. Amino acid-sequence analyses showed that over 90% of the total cell-free product was one homogeneous protein, which corresponds to the MOPC-63 L-chain precursor. In this precursor an extra piece, 20 amino acid residues in length, precedes the N-terminus of the mature L chain. The extra piece contains one methionine residue at the N-terminus, six leucine residues, which are clustered in two triplets at positions 6, 7, 8 and 11, 12, 13, one proline residue at position 16, and one serine residue at position 18. The closely gathered leucine residues, as well as their abundance (30%), suggest that the extra-piece moiety is hydrophobic. In the precursors, the extra piece is coupled to the variable region of the L chain. Partial sequences of precursors of L chains of the same and different subgroups that were labelled with the above six radioactive amino acids indicate that the extra piece is part of the variable region. Thus the precursors of MOPC-63 and MOPC-321 L chains, which are of the same subgroup, have extra pieces of identical size (20 residues), and so far their partial sequences are also identical (see above). On the other hand, in the precursor of MOPC-41 L chain, which is of a different subgroup, the extra piece is 22 residues in length. Further, the sequence of the MOPC-41 extra piece differs in at least ten positions from sequences of the extra pieces of the precursors of MOPC-63 and MOPC-321 L chains.

Sign in / Sign up

Export Citation Format

Share Document