Jove
Visualize
Contact Us

Related Concept Videos

Antibody Structure01:10

Antibody Structure

65.2K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
65.2K
Antibody Structure and Classes01:25

Antibody Structure and Classes

8.2K
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
8.2K
Lampbrush Chromosomes01:51

Lampbrush Chromosomes

8.6K
In 1882, Flemming observed lampbrush chromosomes (LBC) in salamander eggs. Later in 1892, Rückert observed LBCs in shark egg cells and coined the term "lampbrush chromosomes" because they looked like brushes used to clean kerosene lamps.
LBCs are made up of two pairs of conjugating homologous chromatids. Each chromatid consists of alternatively positioned regions of condensed-inactive chromatin and loosely placed-active side loops, which can be contracted and extended. The loops...
8.6K
Evolutionary Relationships through Genome Comparisons02:54

Evolutionary Relationships through Genome Comparisons

6.8K
Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...
6.8K
Protein Families02:47

Protein Families

16.6K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
16.6K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

4.1K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
4.1K
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies
  1. Home
  2. Comparative Analysis Of The Organization And Complexity Of Immunoglobulin Light Chain Loci In Equids.
  1. Home
  2. Comparative Analysis Of The Organization And Complexity Of Immunoglobulin Light Chain Loci In Equids.

Related Experiment Video

Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization
13:55

Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization

Published on: February 3, 2013

18.9K

Comparative analysis of the organization and complexity of immunoglobulin light chain loci in equids.

Yanbo Qiu1, Yichen Lei2, Xiaohua Yi2

  • 1College of Grassland Agriculture, Northwest A&F University, Yangling, Shaanxi, 712100, China.

Journal of Animal Science
|January 9, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

This study characterizes donkey immunoglobulin light-chain (IgL) loci, revealing conserved gene structures and expression patterns across breeds. Findings provide a foundation for developing novel donkey-derived antibody resources.

Keywords:
IGκIGλcomparative analysisdonkeyhorseimmunoglobulin

More Related Videos

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

13.0K
Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation
09:02

Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation

Published on: November 26, 2018

22.3K

Related Experiment Videos

Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization
13:55

Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization

Published on: February 3, 2013

18.9K
Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

13.0K
Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation
09:02

Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation

Published on: November 26, 2018

22.3K

Area of Science:

  • Immunogenetics
  • Comparative Genomics
  • Veterinary Immunology

Background:

  • Immunoglobulin light-chain (IgL) loci structure and diversification are crucial for adaptive immunity.
  • Understanding IgL loci in equids, like donkeys, can inform antibody-based therapeutics.
  • Previous research has not comprehensively detailed the donkey IgL loci.

Purpose of the Study:

  • To characterize the structural organization of donkey immunoglobulin light-chain (IgL) loci (IGλ and IGκ).
  • To investigate diversification mechanisms and expression preferences of donkey IgL loci.
  • To compare donkey IgL loci with those of horses for evolutionary insights.

Main Methods:

  • Genomic DNA sequencing and analysis of three donkey breeds (Guanzhong, Jiami, Northern Shaanxi).
  • Identification and characterization of Vλ, Jλ, Cλ, Vκ, Jκ, and Cκ gene segments.
  • Gene expression profiling to determine light-chain usage biases.
  • Main Results:

    • The donkey IGλ locus on chromosome 8 contains 7 Cλ genes and 156 Vλ genes (29 functional); the IGκ locus on chromosome 6 has 1 Cκ gene, 5 Jκ genes, and 72 Vκ segments (22 functional).
    • Significant light-chain usage preferences were observed, with specific Vλ and Vκ genes/subgroups dominantly expressed.
    • Horses showed similar expression patterns, indicating conserved IgL usage biases within equids.

    Conclusions:

    • Donkey IgL loci exhibit a conserved structure and high conservation of frequently utilized genes and subgroups across breeds.
    • Breed-specific differences in IgL expression are minimal and involve low-frequency genes.
    • This comprehensive elucidation of donkey IgL loci provides a foundation for developing donkey-derived antibody resources.