scholarly journals Sequence diversity within a subgroup of mouse immunoglobulin kappa chains controlled by the IgK-Ef2 locus.

1981 ◽  
Vol 154 (1) ◽  
pp. 146-155 ◽  
Author(s):  
C Lazure ◽  
W T Hum ◽  
D M Gibson
Keyword(s):  
Normal Mouse ◽  
Sequence Diversity ◽  
The Other ◽  
Light Chains ◽  
Chromosome 6 ◽  
Immunoglobulin Kappa ◽  
Mouse Immunoglobulin ◽  
Complete Sequencing ◽  
Polymorphic Bands ◽  
V Region

We previously showed that a chromosome 6 locus, IgK-Ef2, controls a pair of prominent bands in normal mouse light-chain isoelectric focusing profiles. Screening of myeloma light chains derived from BALB/c mice (an IgK-EF2 alpha strain) led to the identification of seven light chains cofocusing with the polymorphic bands controlled by IgK-Ef2. Complete sequencing of the variable (V) regions of four of the light chains indicates that they are all members of the same subgroup (Vk-1A) and they differ from one another by 1--3 substitutions. One of the protein differs from the prototype V-region sequence only in the deletion of a single residue at position 95 immediately preceding of J region. The other two differ from the protype V region by 3 (two framework [fr], one complementarity-determined [cdr]) and one (fr) residues, respectively. Complete V-region sequences of two closely related light chains derived from NZB mice (an IgK-Ef2b strain) indicate the NZB proteins are derived from a distinct Vk gene (Vk-1B), differing by four substitutions from the Vk-1A sequence. The results suggest that the IgK-Ef2 polymorphism may be a result of, at least in part, the loss of the gene(s) coding for the Vk-1A subgroups in IgK-Ef2b strains of mice. The nature of the sequence diversity found in the Vk-1A subgroup indicates that either it is coded by a repeated series of virtually identical genes or that somatic mutation of a single Vk-1A gene may give rise to substitutions in framework as well as cdr regions.

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 Somatic mutation creates diversity in the major group of mouse immunoglobulin kappa light chains.

1984 ◽  
Vol 159 (2) ◽  
pp. 417-435 ◽  
Author(s):  
G Heinrich ◽  
A Traunecker ◽  
S Tonegawa
Keyword(s):  
Somatic Mutations ◽  
Germ Line ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Chromosomal Dna ◽  
Immunoglobulin Kappa ◽  
Hypervariable Regions ◽  
Mouse Immunoglobulin ◽  
Kappa Light Chains ◽  
Cloned Cdna

Using a cloned cDNA of a mouse immunoglobulin kappa light chain synthesized in a myeloma MOPC321 (V kappa-21 subgroup C) as a probe we could detect 13 germ line V kappa gene segments. 11 of these were isolated. Using a set of overlapping cloned segments, we showed that nine of these germ line V kappa genes are arranged in two linkage clusters and that they all have the same transcriptional orientation (11, 12, 22). These two clusters occupy 90 and 30 kb of chromosomal DNA and contain six and three V kappa's, respectively. We determined the complete nucleotide sequences of five germ line V kappa's and showed that three of them encode the prototype sequence of V kappa-21 subgroups B, C, and E. None of these five germ line V kappa's encodes the variant amino acid sequences of known V kappa-21 subgroups. We thus conclude that, as in the lambda 1 light chains, the variant V regions are encoded by gene segments derived by a few somatic mutations from the corresponding germ line DNA. Such somatic mutations are not restricted to sequences encoding the hypervariable regions: they also occur in sequences encoding framework regions.

scholarly journals Sequence Diversity of the Bacillus thuringiensis and B. cereus Sensu Lato Flagellin (H Antigen) Protein: Comparison with H Serotype Diversity

2006 ◽  
Vol 72 (7) ◽  
pp. 4653-4662 ◽  
Author(s):  
Dong Xu ◽  
Jean-Charles Côté
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Nucleotide Sequences ◽  
Amino Acid Sequences ◽  
Sequence Diversity ◽  
The Other ◽  
Bacillus Halodurans ◽  
V Region ◽  
H Serotypes

ABSTRACT We set out to analyze the sequence diversity of the Bacillus thuringiensis flagellin (H antigen [Hag]) protein and compare it with H serotype diversity. Some other Bacillus cereus sensu lato species and strains were added for comparison. The internal sequences of the flagellin (hag) alleles from 80 Bacillus thuringiensis strains and 16 strains from the B. cereus sensu lato group were amplified and cloned, and their nucleotide sequences were determined and translated into amino acids. The flagellin allele nucleotide sequences for 10 additional strains were retrieved from GenBank for a total of 106 Bacillus species and strains used in this study. These included 82 B. thuringiensis strains from 67 H serotypes, 5 B. cereus strains, 3 Bacillus anthracis strains, 3 Bacillus mycoides strains, 11 Bacillus weihenstephanensis strains, 1 Bacillus halodurans strain, and 1 Bacillus subtilis strain. The first 111 and the last 66 amino acids were conserved. They were referred to as the C1 and C2 regions, respectively. The central region, however, was highly variable and is referred to as the V region. Two bootstrapped neighbor-joining trees were generated: a first one from the alignment of the translated amino acid sequences of the amplified internal sequences of the hag alleles and a second one from the alignment of the V region amino acid sequences, respectively. Of the eight clusters revealed in the tree inferred from the entire C1-V-C2 region amino acid sequences, seven were present in corresponding clusters in the tree inferred from the V region amino acid sequences. With regard to B. thuringiensis, in most cases, different serovars had different flagellin amino acid sequences, as might have been expected. Surprisingly, however, some different B. thuringiensis serovars shared identical flagellin amino acid sequences. Likewise, serovars from the same H serotypes were most often found clustered together, with exceptions. Indeed, some serovars from the same H serotype carried flagellins with sufficiently different amino acid sequences as to be located on distant clusters. Species-wise, B. halodurans, B. subtilis, and B. anthracis formed specific branches, whereas the other four species, all in the B. cereus sensu lato group, B. mycoides, B. weihenstephanensis, B. cereus, and B. thuringiensis, did not form four specific clusters as might have been expected. Rather, strains from any of these four species were placed side by side with strains from the other species. In the B. cereus sensu lato group, B. anthracis excepted, the distribution of strains was not species specific.

scholarly journals Molecular characterization of some selected persimmon genotypes and cultivars by srap and ssr markers

Genetika ◽  
2017 ◽  
Vol 49 (2) ◽  
pp. 693-704
Author(s):  
Hasan Pinar ◽  
Ercan Yildiz ◽  
Mustafa Kaplankiran ◽  
Celil Toplu ◽  
Mustafa Unlu ◽  
...  
Keyword(s):  
Ssr Markers ◽  
Clonal Propagation ◽  
Genetic Relationships ◽  
The Other ◽  
Diospyros Kaki ◽  
Ssr Primers ◽  
Similarity Ratio ◽  
Polymorphic Bands ◽  
Dna Primers

In this study, SRAP and SSR markers were employed to determine genetic relationships among 42 persimmon genotypes (Diospyros kaki Thunb) obtained from Hatay province and 3 persimmon cultivars, 2 of which belong to Diospyros kaki Thunb and one belongs to Diospyros oleifera Cheng. Genetic relationships were determined by using a total of 29 molecular DNA primers (SRAP and SSR). Of these primers, 21 SRAP primer combinations produced a total of 107 bands and 77.6% of them were polymorphic; 8 SSR primers produced 26 polymorphic bands with an average polymorphism ratio of 84.6%. The SRAP and SSR markers produced 4.6 bands as average and the number of bands produced per marker was calculated as 3.6. The lowest similarity was observed between MK-113 (Diospyros oleifera Cheng) and the other genotypes all belongs to Diospyros kaki Thunb (with similarity ratios of 0.41-0.69 for SRAP primers, between 0.25-0.67 for SSR primers). The genotypes/cultivars belongs to Diospyros kaki had similarity ratio between 0.98-1.00 according to SRAP and SSR markers. This synonym or similarity could be results of clonal propagation rather than autogamy.

Translation of messenger RNA for mouse immunoglobulin light chains in living frog oocytes

1973 ◽  
Vol 80 (3) ◽  
pp. 553-557 ◽  
Author(s):  
M. Smith ◽  
J. Stavnezer ◽  
R.C. Huang ◽  
J.B. Gurdon ◽  
C.D. Lane
Keyword(s):  
Messenger Rna ◽  
Light Chains ◽  
Immunoglobulin Light Chains ◽  
Mouse Immunoglobulin

scholarly journals A complex translocation at the murine kappa light-chain locus.

1987 ◽  
Vol 7 (11) ◽  
pp. 4130-4133 ◽  
Author(s):  
M A Shapiro ◽  
M Weigert
Keyword(s):  
Light Chain ◽  
Chromosome 12 ◽  
Chromosome 15 ◽  
Chromosome 6 ◽  
Kappa Light Chain ◽  
Complex Translocation ◽  
Immunoglobulin Kappa ◽  
Complex Series ◽  
Chain Locus ◽  
Light Chain Locus

We have previously reported that a segment of DNA from a murine plasmacytoma comprises DNA from three chromosomes, the immunoglobulin kappa light-chain locus on chromosome 6, the S mu locus on chromosome 12, and a region on chromosome 15. We now report that the reciprocal product contains DNA from only the kappa locus and chromosome 15 and not from S mu. We conclude that a complex series of events, including both a transposition of DNA and a translocation between chromosomes, generated these imperfect reciprocal products.

scholarly journals Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment

1968 ◽  
Vol 106 (1) ◽  
pp. 15-21 ◽  
Author(s):  
B. Frangione ◽  
C. Milstein ◽  
Edward C. Franklin
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
The Other ◽  
Light Chains ◽  
Fc Fragment ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Other Hand ◽  
Terminal Loop ◽  
Heavy Chain Disease

The disulphide bridges of the Fc fragment (C-terminal half of the heavy chain) have been studied in several human immunoglobulins, containing heavy chains of different antigenic types (γ1, γ2, γ3 and γ4), and in heavy-chain-disease proteins. Two intrachain disulphide bridges were found to be present. The sequences appear to be identical in the Fc fragments of two types of chain studied (γ1 and γ3), and very similar to corresponding sequences of the Fc fragment in rabbit. These results suggest that the C-terminal half of the heavy chains is covalently folded (in a similar fashion to the light chains) with a C-terminal loop and an N-terminal loop. The similarity is emphasized by comparison of the sequence and location of the disulphide-bridged peptides of the C-terminal loop of heavy and light chains. The N-terminal loop, on the other hand, appears to be very different in Fc fragments and light chains. The C-terminal loop is the only one present in the F′c fragment.

scholarly journals AN IDIOTYPIC CROSS-REACTION BETWEEN ALLOTYPE a3 AND ALLOTYPE a NEGATIVE RABBIT ANTIBODIES TO STREPTOCOCCAL CARBOHYDRATE

1973 ◽  
Vol 137 (3) ◽  
pp. 636-648 ◽  
Author(s):  
Thomas J. Kindt ◽  
David G. Klapper ◽  
Michael D. Waterfield
Keyword(s):  
Chemical Analysis ◽  
Cross Reaction ◽  
The Other ◽  
Light Chains ◽  
Binding Affinities ◽  
Variable Regions ◽  
Heavy Chains ◽  
Relative Binding ◽  
Group A

Two antibodies to Group C streptococcal carbohydrate isolated from an individual rabbit had similar relative binding affinities for a Group C immuno-adsorbent column. Their light chains were similar, if not identical, as were the constant regions of their heavy chains. Differences in the variable regions of the H chains of the two antibodies were detected by chemical analysis. The two antibodies had serologically identical idiotypic determinants although one antibody possessed the a3 allotype and the other had no detectable group a marker. The occurrence of such antibodies indicates the absence of obligatory associations between group a allotypes and idiotypic specificities, despite the fact that both determinants have antigenic components in the VH region of the H chain.

scholarly journals Interchain disulphide bridges of mouse immunoglobulin M

1975 ◽  
Vol 151 (3) ◽  
pp. 615-624 ◽  
Author(s):  
C P Milstein ◽  
N E Richardson ◽  
E V Dieverson ◽  
A Feinstein
Keyword(s):  
Selective Reduction ◽  
Terminal Region ◽  
Immunoglobulin M ◽  
The Other ◽  
Mouse Immunoglobulin

Mouse IgM (immunoglobulin M) was selectively and partially reduced and treated with iodo[2-14C]acetate to label the interchain disulphide bridges. The carboxymethylation was studied in some detail. The labelled peptides were purified, sequenced and positioned by homology with human IgM. Only peptides originating from three interchain disulphide bridges were labelled, in contrast with the four labelled bridges obtained in human IgM under the same conditions. These peptides are homologous to human bridge peptides forming the heavy-light bridge and two inter-heavy bridges, one present in the Cμ2 region and the other in the C-terminal region. The inter-heavy bridge in the Cμ2 region was alone cleaved and radioactively labelled in selectively reduced IgM held together as a pentamer by non-covalen interactions. The same bridge was the only one to be totally cleaved in subunits released after more extensive, though still selective, reduction. In the light of these results a possible arrangement of the disulphide bridges of the mouse IgM pentamer is proposed.

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