scholarly journals ENTIERE IDENTITIES BETWEEN OPHIOCOMINA NIGRA IGKAPPA GENE AND HUMAN IMMUNOGLOBULIN KAPPA LOCUS.NEW ASPECTS OF INVERTEBRATE IGKAPPA GENES (IPA)

2020 ◽  
pp. 53-55
Keyword(s):  
De Novo ◽  
Human Immunoglobulin ◽  
Original Sequence ◽  
Immunoglobulin Kappa

Entiere identities between Invertebrate Ophiocomina nigra IGKappa gene and Human IGK gene are confirmed, in the present work, at the level of immunoglobulin domains (constant and variable). The transcriptome of the Ophuirid : Ophiocomina nigra IGKappa gene was discovered recently(1).Since it was synthesized de novo and cloned in a pUC-GW-Kan plasmid (2) which was a gift of Bo Huang laboratories. The original sequence of the IGKappa gene, after cloning, was the following in 5’-3’ :

scholarly journals Significant Differences in Physicochemical Properties of Human Immunoglobulin Kappa and Lambda CDR3 Regions

2016 ◽  
Vol 7 ◽  
Author(s):  
Catherine L. Townsend ◽  
Julie M. J. Laffy ◽  
Yu-Chang Bryan Wu ◽  
Joselli Silva O’Hare ◽  
Victoria Martin ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Human Immunoglobulin ◽  
Immunoglobulin Kappa

scholarly journals B-cell nuclear proteins binding in vitro to the human immunoglobulin kappa enhancer: localization by exonuclease protection.

1987 ◽  
Vol 7 (5) ◽  
pp. 1815-1822 ◽  
Author(s):  
J M Gimble ◽  
D Levens ◽  
E E Max
Keyword(s):  
Protein Binding ◽  
B Cell ◽  
Base Pair ◽  
Consensus Sequence ◽  
Dimethyl Sulfate ◽  
Simian Virus 40 ◽  
Human Immunoglobulin ◽  
Core Element ◽  
Immunoglobulin Kappa

Proteins capable of interacting with the enhancer of the immunoglobulin kappa gene in vitro have been detected in extracts of nuclei from human B cells and from human, mouse, and rabbit spleens. The experiments, based on an exonuclease protection technique, demonstrate nuclear protein factors binding to a 30- to 35-base-pair domain containing both the simian virus 40 enhancer core element (TTTCCA) and the octamer CAGGTGGC that was previously identified as the consensus sequence for protein-binding sites in the murine immunoglobulin heavy-chain enhancer. This 30- to 35-base-pair domain in the human kappa enhancer is homologous to a site of protein binding detected in the murine kappa enhancer by other investigators using a gel retardation assay. Our results complement in vivo dimethyl sulfate footprinting studies of the human immunoglobulin kappa enhancer which demonstrated B cell-specific changes in guanine reactivity immediately 5' to the consensus octamer. Together, these findings suggest that DNA-binding proteins in B-cell nuclei interact with the 5' portion of the human kappa-gene enhancer. Such proteins could play a role in the B cell-specific transcription of the human immunoglobulin kappa gene.

scholarly journals SacI RFLP recognized by a human immunoglobulin kappa light chain constant region probe

1987 ◽  
Vol 15 (9) ◽  
pp. 3942-3942 ◽  
Author(s):  
L.L. Field ◽  
R. Tobias ◽  
T. Bech-Hansen
Keyword(s):  
Light Chain ◽  
Human Immunoglobulin ◽  
Constant Region ◽  
Kappa Light Chain ◽  
Immunoglobulin Kappa

scholarly journals A human immunoglobulin kappa orphon without sequence defects may be the product of a pericentric inversion

1990 ◽  
Vol 18 (12) ◽  
pp. 3475-3478 ◽  
Author(s):  
Christian Huber ◽  
Rainer Thiebe ◽  
Horst Hameister ◽  
Hans Smola ◽  
Erika Lötscher ◽  
...  
Keyword(s):  
Pericentric Inversion ◽  
Human Immunoglobulin ◽  
Immunoglobulin Kappa

scholarly journals Characterization of the human immunoglobulin kappa gene 3' enhancer: functional importance of three motifs that demonstrate B-cell-specific in vivo footprints.

1992 ◽  
Vol 12 (11) ◽  
pp. 5206-5216 ◽  
Author(s):  
J G Judde ◽  
E E Max
Keyword(s):  
T Cell ◽  
B Cell ◽  
Regulatory Elements ◽  
Human Immunoglobulin ◽  
Site Directed Mutagenesis ◽  
Cooperative Interaction ◽  
Enhancer Element ◽  
Immunoglobulin Kappa ◽  
In Vivo Footprinting

Using a combination of in vivo footprinting and site-directed mutagenesis, we have functionally characterized an enhancer located 12 kb downstream of the human immunoglobulin kappa constant-region gene. The core enhancer region is highly homologous to the murine 3' kappa enhancer. However, in addition to two regulatory elements homologous to the functional motifs of the murine enhancer, we find a third positive regulatory element in the human enhancer. This element is associated with an 11/12-bp direct repeat (DR) that is well conserved in the murine locus but was not recognized as functionally important in the murine enhancer. Mutation of any of the three motifs of the human enhancer decreases its activity to 3 to 20% of the wild-type level, indicating cooperative interaction between these elements. The DR motif does not resemble any known enhancer element and does not appear to function as a transcriptional activator on its own when present in multiple copies. Interestingly, nuclear extracts from both B- and T-cell lines contain factors binding to DR in vitro, but in vivo footprinting shows no evidence of protein-DNA binding in the T-cell line. This finding suggests that an additional regulatory mechanism, such as the effect of chromatin configuration on accessibility, may be involved in the B-cell-restricted activity of the human 3' kappa enhancer.

scholarly journals Identification and partial purification of a protein binding to the human immunoglobulin kappa enhancerxE2 site

1988 ◽  
Vol 16 (11) ◽  
pp. 4967-4988 ◽  
Author(s):  
Jeffrey M. Gimble ◽  
James R. Flanagan ◽  
David Recker ◽  
Edward E. Max
Keyword(s):  
Protein Binding ◽  
Human Immunoglobulin ◽  
Partial Purification ◽  
Immunoglobulin Kappa
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