scholarly journals Glycopeptides from human χ-chains

1971 ◽  
Vol 121 (2) ◽  
pp. 211-215 ◽  
Author(s):  
Celia P. Milstein ◽  
C. Milstein
Keyword(s):  
Attachment Site ◽  
Variable Region ◽  
Light Chains ◽  
Myeloma Proteins

Glycopeptides have been isolated from tryptic digests of κ-type light chains separated from human myeloma proteins obtained from the serum of two patients, Car and Rai. The glycopeptides are derived from the variable region of the chain in both cases, but from different sections. On the basis of homology it is deduced that glycopeptide from Car, κI type, is derived from position 25–31 whereas that from Rai, κII type, is from position 62–77, their sequences being respectively Ala-Ser-Gln-Asn-Ile-Ser and Phe-Ser-Gly-Ser-Gly-Ser-Gly(Thr,Asp)Phe-Thr-Leu-Asx-Ile-Ser-Arg. The significance of the results is discussed in connexion with the nature of the attachment site of carbohydrate to protein.

scholarly journals A major group of mouse kappa chains controlled by the chromosome 6 locus, IgK-Ef2.

1980 ◽  
Vol 152 (3) ◽  
pp. 555-564 ◽  
Author(s):  
C Lazure ◽  
W T Hum ◽  
D M Gibson
Keyword(s):  
Light Chain ◽  
Normal Mouse ◽  
Variable Region ◽  
Normal Serum ◽  
Light Chains ◽  
Mouse Serum ◽  
Chromosome 6 ◽  
Frequency Of Occurrence ◽  
Myeloma Proteins ◽  
Normal Light

We previously demonstrated that loci closely linked to the Ly-3 locus control the expression of distinct sets of light chains in normal mouse serum immunoglobulin. One of these loci, IgK-Ef2, was shown to control two major bands in normal light chain isoelectric focusing (IF) profiles. Strains possessing the marker bands were designated IgK-Ef2a. Screening of myeloma proteins from the strains BALB/c (IgK-Ef2a) and NZB (IgK-Ef2b) led to the identification of eight proteins in the BALB/c collection having light chains that cofocus precisely with the polymorphic IF bands observed in normal serum light chains. Partial sequence analysis of 3 of the light chains has shown that they are all identical in the first 30 positions, which indicates that they constitute a single variable region of the kappa light chain (VK) group (VK1). The frequency of occurrence of the group within the BALB/c myeloma collections (8 out of 277) suggests that the number of such groups may be closer to 50 than to 100. The finding supports an interpretation of the genetic polymorphism as being in part a result of the absence of genes related to VK1 in IgK-Ef2b strains of mice.

scholarly journals The specificity of chain interactions among immunoglobulins. Combinations of γ chains with κ chains of the same subgroup as in the parent immunoglobulin G

1974 ◽  
Vol 139 (2) ◽  
pp. 369-374 ◽  
Author(s):  
G. T. Stevenson ◽  
L. E. Mole
Keyword(s):  
Immunoglobulin G ◽  
Structural Information ◽  
Variable Region ◽  
Light Chains ◽  
Predominant Role ◽  
Variable Regions ◽  
Human Immunoglobulins ◽  
Myeloma Proteins ◽  
Standard Population ◽  
Normal Light

1. The specificity of combination of heavy and light chains from selected human immunoglobulins was examined in the light of greater structural information than in previous studies. Heavy (γ) chains from immunoglobulin G (κ) myeloma proteins were allowed to combine with their homologous light (κ) chains or with other κ chains of the same variable-region subgroup. The affinity of each such pairing was assessed by having the test κ chain compete with a standard population of normal light chains. 2. There was a spread of affinities among the heavy–light pairings with the homologous pairings having an average affinity significantly higher than the heterologous pairings. 3. It follows that (a) the preference shown for homologous heavy–light pairings is not explicable simply in terms of the known subdivisions of the variable and constant regions of the chains, and (b) it is unlikely that those residues specifying the subgroups of κ-chain variable regions have a predominant role in the formation of interchain bonds with the γ-chain variable regions.

scholarly journals Idiotypes of inulin-binding myeloma proteins localized to variable region light and heavy chains: genetic significance.

1977 ◽  
Vol 146 (5) ◽  
pp. 1294-1304 ◽  
Author(s):  
R Lieberman ◽  
M Vrana ◽  
W Humphrey ◽  
C C Chien ◽  
M Potter
Keyword(s):  
Variable Region ◽  
Light Chains ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Genetic Significance

Idiotypes of inulin-binding myeloma proteins (InuBMP) were determined primarly by variable region light chains (VL) or by variable region heavy chains (VH) but needed both chains to be expressed. Recombinant molecules were used to show that individual idiotypes (IdI) of U61, E109, T957, and A4 InuBMP and cross-specific idiotypes (IdXB) of U61 were primarily determined by VL while cross-specific idiotype (IdXA) of A4 was determined mainly by VH. The assignment of genes controlling idiotypes to VH based on allotype linkage (e.g., IdXB) is dubious until the role of the L chain in determining that idiotype is assessed. IdXB has been shown to be a VL-VH marker which presumably is controlled by two unlinked genes. However IdXB can be used as a L chain marker in combinations of strains differing in their L chain genes but having the same permissive H chain genes. Conversely IdXB can be used as a H chain marker in strains having the same permissive L chain genes but differing in their H chain genes.

scholarly journals Restricted diversity of the variable region nucleotide sequences of the heavy and light chains of a human rheumatoid factor

1991 ◽  
Vol 34 (3) ◽  
pp. 343-350 ◽  
Author(s):  
Ichiko Ezaki ◽  
Masao Shingu ◽  
Masashi Nobunaga ◽  
Hidetoshi Kanda ◽  
Takeshi Watanabe ◽  
...  
Keyword(s):  
Rheumatoid Factor ◽  
Variable Region ◽  
Nucleotide Sequences ◽  
Light Chains

scholarly journals Variable region sequences of murine IgM anti-IgG monoclonal autoantibodies (rheumatoid factors). A structural explanation for the high frequency of IgM anti-IgG B cells.

1986 ◽  
Vol 164 (2) ◽  
pp. 407-427 ◽  
Author(s):  
M J Shlomchik ◽  
D A Nemazee ◽  
V L Sato ◽  
J Van Snick ◽  
D A Carson ◽  
...  
Keyword(s):  
B Cells ◽  
Variable Region ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Binding Interaction ◽  
Structural Explanation ◽  
Region Gene ◽  
Unique Type ◽  
Heavy Chains ◽  
Germline Genes

The nucleotide sequences of heavy and light chains from 10 monoclonal IgM anti-IgG1 (RF) antibodies were determined and reported here as translated amino acid sequences. Only three families of VK light chains were used in these antibodies: VK1 (two examples), VK8 (three examples), and VK19 (four examples). This represents a significant nonrandom selection of light chains. In contrast, all other variable region gene segments (i.e., VH, DH, JH, and JK) were used in a pattern consistent with random selection from the available pool of germline genes. In two cases, the same anti-IgG1 specificity was generated by a combination of very homologous light chains with unrelated heavy chains. We infer from this that the light chain is the segment used by these antibodies to bind IgG1. The nature of these sequences provides an explanation for the curious observation that as many as 15% of splenic B cells in normal mice may be expressing IgM anti-IgG; if, as our data suggest, certain light chains in combination with many different heavy chains can be used in assembling the anti-IgG specificity, then, because of combinatorial association in which the heavy chain is not relevant for specificity, the fraction of IgM-producing B cells expressing these light chains should approximate the fraction of B cells making IgM anti-IgG. We calculate, based on data presented in several other studies, that 5-17% of B cells express one of the VK types observed in monoclonal RF. This agrees well with estimates for the number of B cells making IgM anti-IgG. In addition, our findings could rule out other explanations of the high percentage of B cells making RF, such as constant stimulation by antigen or presence of numerous antigenic epitopes since it was shown that IgM anti-IgG1 antibodies are not somatically mutated and that they are structurally homogeneous. We aligned the VK sequences of the RF in hopes of finding some primary sequence homology between the represented VK families which might point to residues involved in the binding interaction. Although we found no such homology in the hypervariable regions, we did find significant and unexpected homology in the FR2 and FR3 of these light chains. We noted that these regions are exposed in the Ig structure and postulate that they may be involved in a unique type of binding interaction between two Ig family domains, i.e., VK binding to a constant region domain of IgG.

scholarly journals Loss of an individual idiotype on chemical modification. A strategy for assigning idiotypic determinants.

1981 ◽  
Vol 153 (5) ◽  
pp. 1275-1285 ◽  
Author(s):  
J Dickerman ◽  
B Clevinger ◽  
B Friedenson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Chemical Modification ◽  
Heavy Chain ◽  
Light Chains ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Low Levels ◽  
The Individual ◽  
Complementary Strategy

Two dextran-binding myeloma proteins, J558 and Hdex 24, which possess the same individual idiotype (IdI) were diazotized to low levels (1-3.3 groups per subunit) with 1-[14C]-p-aminobenzoate. Both proteins lost the IdI idiotype under these conditions with most of the label incorporated on the heavy chains of each protein. When the diazotization ws carried out in the presence of the hapten 1-O-methyl-alpha-D-glucopyranoside the loss of idiotypic reactivity could be prevented for J558 but not for Hdex 24. Under these conditions most of the label was incorporated on the light chains of J558, but on the heavy chains of Hdex 24. For J558, these results show that a major determinant of the individual idiotype is within the hypervariable positions of the heavy chain. For Hdex 24 the determinant being modified is on the heavy chain but not involved in hapten binding. These results are consistent with previous work showing that J558 and Hdex 24 differ in amino acid sequence in the D and the J segments of the heavy chain and offer an alternative and complementary strategy for assigning idiotypic determinants.

scholarly journals AN ANALYSIS OF THE SEQUENCES OF THE VARIABLE REGIONS OF BENCE JONES PROTEINS AND MYELOMA LIGHT CHAINS AND THEIR IMPLICATIONS FOR ANTIBODY COMPLEMENTARITY

1970 ◽  
Vol 132 (2) ◽  
pp. 211-250 ◽  
Author(s):  
Tai Te Wu ◽  
Elvin A. Kabat
Keyword(s):  
Sequence Data ◽  
Variable Region ◽  
High Variability ◽  
Light Chains ◽  
Variable Regions ◽  
Advantages And Disadvantages ◽  
Specific Subgroup ◽  
Species Specific ◽  
Specific Species ◽  
Bence Jones Proteins

In an attempt to account for antibody specificity and complementarity in terms of structure, human κ-, human λ-, and mouse κ-Bence Jones proteins and light chains are considered as a single population and the variable and constant regions are compared using the sequence data available. Statistical criteria are used in evaluating each position in the sequence as to whether it is essentially invariant or group-specific, subgroup-specific, species-specific, etc. Examination of the invariant residues of the variable and constant regions confirms the existence of a large number of invariant glycines, no invariant valine, lysine, and histidine, and only one invariant leucine and alanine in the variable region, as compared with the absence of invariant glycines and presence of three each of invariant alanine, leucine, and valine and two each of invariant lysine and histidine in the constant region. The unique role of glycine in the variable region is emphasized. Hydrophobicity of the invariant residues of the two regions is also evaluated. A parameter termed variability is defined and plotted against the position for the 107 residues of the variable region. Three stretches of unusually high variability are noted at residues 24–34, 50–56, and 89–97; variations in length have been found in the first and third of these. It is hypothesized that positions 24–34 and 89–97 contain the complementarity-determining residues of the light chain—those which make contact with the antigenic determinant. The heavy chain also has been reported to have a similar region of very high variability which would also participate in forming the antibody-combining site. It is postulated that the information for site complementarity is contained in some extrachromosomal DNA such as an episome and is incorporated by insertion into the DNA of the structural genes for the variable region of short linear sequences of nucleotides. The advantages and disadvantages of this hypothesis are discussed.

Nucleotide sequence of the variable region of the heavy and light chains of a monoclonal IgG antibody reactive to herbicides, terbutryn and prometryn

DNA Sequence ◽  
1995 ◽  
Vol 6 (1) ◽  
pp. 51-54 ◽  
Author(s):  
Sabine B. Kreissig ◽  
Vernon K. Ward ◽  
Bruce D. Hammock ◽  
Prabhakara V. Choudary
Keyword(s):  
Nucleotide Sequence ◽  
Variable Region ◽  
Light Chains ◽  
Igg Antibody
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