IgM antibody–I. Heterogeneity of the component chains of equine anti-lactose antibody.
Abstract: The heterogeneity of the IgM response has been studied with anti-lactose antibody purified from the sera of seven horses. The IgM antibody was induced with a bacterial vaccine and the sera were obtained during a one-year period of immunization. L and H chain preparations were derived from separate bleedings of each horse and examined by analytical isoelectric focusing. All of the L chain preparations were complex and similar and, under optimum conditions, exhibited about 45 bands. Their similarity included almost identical concentration distributions over the entire pH gradient. Isoelectric bands due to J chains could also be identified at the acidic end of the gradient. The H chain preparations also showed very similar patterns which were limited to the relatively narrow pH range of 5.4–6.2. Only 10 distinct bands could be recognized. The striking similarity within the H chain populations and the L chain populations, including preparations from IgM without anti-lactose specificity, suggest that the isoelectric pattern is primarily due to the isoelectric distribution of the major subgroups of both μ and L chains. The implications of these findings for the notion that IgM is specified by structural genes acquired by inheritance is examined. It is pointed out that the system described here provides an experimental approach to this proposal.
Publication Date: 1977-03-01 PubMed ID: 16825DOI: 10.1016/0019-2791(77)90189-6Google Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov\'t
- P.H.S.
Summary
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This research investigates the varied nature of the IgM immune response, particularly in relation to antibodies against lactose, with a focus on the similarities and differences observed in L and H chain preparations of these antibodies.
Research Background
- The immunoglobulin M (IgM) response plays a crucial role in the immune response, and understanding its behavior is key to improving knowledge of immune function.
- The research investigated the heterogeneity of the IgM immune response, specifically with regard to anti-lactose antibodies.
- These antibodies were obtained from the blood serum of horses who were immunized with a bacterial vaccine over the course of a year.
Methods and Findings
- The researchers derived L (light) and H (heavy) chain preparations from separate horse blood samples. These are types of polypeptides (protein chains) that constitute an antibody.
- Analytical isoelectric focusing was applied to examine these samples. This is a procedure used to determine the isoelectric point (pI), the pH at which a molecule carries no net electric charge.
- The L chain preparations showed complexity and similarity across samples, displaying about 45 different bands under optimal conditions. Their pattern distribution was almost identical across the entire pH scale.
- At the acidic end of the gradient, certain isoelectric bands were identifiable as J chains, which are another component of particular antibodies.
- The H chain preparations showed a narrower range of pH (5.4–6.2) and exhibited about 10 distinct bands, showing much similarity within the H chain populations.
- Even among preparations from IgM antibodies without anti-lactose specificity, there was striking similarity within both L and H chain populations, suggesting the distribution is primarily due to the isoelectric properties of major subgroups of these chains.
Implications and Further Research
- The findings provide insight into the heterogeneity of IgM immune responses, bringing into question the belief that IgM is specified by inherited structural genes.
- Researchers mention that the system described in this study could furnish an experimental approach to further investigate this proposal.
Cite This Article
APA
Mitchell KF, Karush F, Morgan DO.
(1977).
IgM antibody–I. Heterogeneity of the component chains of equine anti-lactose antibody.
Immunochemistry, 14(3), 161-164.
https://doi.org/10.1016/0019-2791(77)90189-6 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Antibodies / analysis
- Horses
- Hydrogen-Ion Concentration
- Immunoglobulin Heavy Chains
- Immunoglobulin Light Chains
- Immunoglobulin M / analysis
- Isoelectric Focusing
- Lactose / immunology
Citations
This article has been cited 2 times.- Pazur JH, Liu B, Witham TF. Isolation and characterization of sets of anti-L-fucose and anti-bovine serum albumin antibodies directed against a glycoconjugate of L-fucose and bovine serum albumin. J Protein Chem 1994 Jan;13(1):59-66.
- Allen PZ, Glode M, Schneerson R, Robbins JB. Identification of immunoglobulin heavy-chain isotypes of specific antibodies of horse 46 group B meningococcal antiserum. J Clin Microbiol 1982 Feb;15(2):324-9.
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