Results 341 to 350 of about 172,498 (401)

Immunoglobulin heavy chains in medaka (Oryzias latipes)

open access: yes, 2011
Gambón Deza, Francisco   +1 more
openaire   +1 more source
Some of the next articles are maybe not open access.

Related searches:

Hypervariable region of human immunoglobulin heavy chains.

Nature New Biology, 1971
THE variable regions of human immunoglobulin light chains contain three areas of unusually high variability1–4. Similar hypervariable regions have been postulated for human heavy chains5, 6, but there are no amino-acid sequence data to support this idea.
J. Capra
semanticscholar   +3 more sources

Immunoglobulin heavy chain binding protein

Nature, 1983
Pre-B lymphocytes, and hybridomas derived from them, synthesize immunoglobulin heavy (IgH) chain in the absence of light (L) chain. In the Abelson virus transformed line 18-81, which is representative of the pre-B cell stage, we observed that at least some of the H-chains are bound to a protein other than L-chain.
Haas, I., Wabl, M.
openaire   +3 more sources

The immunoglobulin heavy chain class switch

Molecular and Cellular Biochemistry, 1984
While much has been learned concerning the molecular structural basis for the heavy chain class switch, many questions relating to the regulation of the switch remain unanswered, or at least controversial. Identification of the enzyme system which mediates the class switch, as well as other regulatory, possibly X-linked, genes should provide the ...
P D, Burrows, M D, Cooper
openaire   +2 more sources

Origins of immunoglobulin heavy chain domains

Journal of Molecular Evolution, 1980
Using computer programs that analyze the evolutionary history and probability of relationship of protein sequences, we have investigated the gene duplication events that led to the present configuration of immunoglobulin C regions, with particular attention to the origins of the homology regions (domains) of the heavy chains.
W C, Barker, L K, Ketcham, M O, Dayhoff
openaire   +2 more sources

Whale immunoglobulins—II. Heavy chain structure

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1972
Abstract 1. 1. Immunoglobulins (7S) were purified from the plasmas of three species of whales, hump-backed, fin-backed and Sei. 2. 2. Heavy polypeptide chains were characterized and compared to human γ chains. 3. 3. Amino acid composition and peptide map comparisons indicated much homology between the whale 7S Ig heavy chain and hyman γ.
J C, Travis, B G, Sanders
openaire   +2 more sources

Rat immunoglobulin E heavy chain locus

Journal of Molecular Biology, 1984
A 2100 base-pair long sequence has been established which covers all four constant domains of the rat epsilon-chain. An analysis of messenger RNA from an immunoglobulin E producing rat immunocytoma revealed two separate epsilon-chain mRNA species, 2.3 X 10(3) and 2.8 X 10(3) base-pairs long.
M L, Steen, L, Hellman, U, Pettersson
openaire   +2 more sources

Immunoglobulin heavy-chain loci in ancient allotetraploid goldfish

Developmental & Comparative Immunology, 2022
As an ancient allotetraploid species, goldfish (Carassius auratus) have two sets of subgenomes. In this study, immunoglobulin heavy-chain (IGH) genes were cloned from the red crucian carp (Carassius auratus red var.), and the corresponding loci were identified in the gynogenetic diploid red crucian carp (GRCC) genome as well as the genomes of three ...
Linmei, Han   +12 more
openaire   +2 more sources

Regulation of immunoglobulin heavy‐chain gene rearrangements

Immunological Reviews, 2004
Summary:  Regulated assembly of antigen receptor gene segments to produce functional genes is a hallmark of B‐ and T‐lymphocyte development. The immunoglobulin heavy‐chain (IgH) and T‐cell receptor β‐chain genes rearrange first in B and T lineages, respectively.
Dipanjan, Chowdhury, Ranjan, Sen
openaire   +2 more sources

Immunoglobulin heavy-chain constant-region genes

Cell, 1982
Antibodies are composed of two identical heavyand light-chain polypeptides. Each heavy and light chain contains an amino-terminal variable (V) region, responsible for antigen recognition, and a carboxy-proximal constant(C) region, which participates in a variety of immunological processes, including effector-cell recognition and complement fixation ...
openaire   +2 more sources

Home - About - Disclaimer - Privacy