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Topic:Immunoglobulin A

Immunoglobulin A (IgA) is an antibody that plays a significant role in the mucosal immunity of horses. It is primarily found in mucous membranes lining the respiratory, gastrointestinal, and urogenital tracts, as well as in secretions such as saliva and tears. IgA functions by binding to pathogens and preventing their adherence to and penetration of mucosal surfaces. This antibody is a key component of the horse's immune system, providing a first line of defense against environmental pathogens. Research on equine IgA focuses on its production, distribution, and function, as well as its potential use as a biomarker for disease susceptibility and immune status in horses. This page gathers peer-reviewed research studies and scholarly articles that explore the role, mechanisms, and clinical implications of immunoglobulin A in equine health.
N-Terminal sequences of equine and human immunoglobulin heavy chains.
Biochimica et biophysica acta    February 17, 1970   Volume 200, Issue 2 258-266 doi: 10.1016/0005-2795(70)90169-8
Montgomery PC, Bello AC, Rockey JH.N-terminal tetrapeptides from heavy chains of equine γGab- and γT-globulins, and of human γG and γA myeloma proteins and a γM macroglobulin, have been studied. The equine and human heavy chains lacked free α-amino-terminal groups. After mild alkaline hydrolysis, glutamic acid was identified as the terminal amino acid by reaction with dimethylaminonaphthalenesulfonyl chloride, tentatively identifying pyrrolid-2-one-5-carboxylic acid (PCA) as the unreactive terminal residue of each heavy chain. Peptides lacking a free α-amino group were isolated from subtilisin and pronase digests of the ...
The response of ponies to Myxovirus influenzae A-equi 2. II. Immunoglobulin classes of antibody to the virus in serum and nasal secretions. Rouse BT, Ditchfield WJ.Nasal secretions and serum were collected from ponies in order to determine the types of immunoglobulins responsible for antibody activity against Myxovirus influenzae A-equi 2. Using specific antisera to remove each immunoglobulin, the antiviral activity of serum was shown to be a property of IgG globulin, whereas in nasal secretions activity was found in both IgG and IgG(T) globulins. However in secretions the predominant activity was attributed to IgG(T) globulin. Because of its sensitivity to 2 mercaptoethanol, early serum antibody was assumed to belong to the IgM class of immunoglobulins....
Comparison of the structure of the immunoglobulins from horse serum.
The Biochemical journal    July 1, 1966   Volume 100, Issue 1 63-68 doi: 10.1042/bj1000063
Weir RC, Porter RR.A study of the chemical structure of the horse immunoglobulins IgG and IgA(T) has shown that the amino acid contents of the peptide chains are very similar. These globulins differ most markedly in the products of papain digestion. IgG gives 3.5s products, whereas IgA(T) gives a 5s fraction and smaller components. This difference appears to be associated with the presence of an additional easily reducible disulphide bond in the Fd fragment of the heavy chain. There is two to three times as much carbohydrate in IgA(T) as in IgG. In both, this is in the heavy chain and in IgA(T) more than half is...
The alexination and conglutination reactions. The reactions between sensitized erythrocytes and horse complement and between alexinated erythrocytes and conglutinin.
Immunology    July 1, 1962   Volume 5, Issue 4 511-521 
INGRAM DG.A method is described for the quantitative measurement of the reactions between sensitized cells and horse complement and between alexinated cells and conglutinin. The method is laborious but its application has allowed the determination of the optimal times of the reactions at various temperatures. The results obtained in these experiments indicate that the alexinated configuration with which conglutinin and immuno-conglutinin react is not one of the recognized intermediates formed during the process of immune haemolysis.
[Ninhydrin and antigen-antibody reaction. I. Effect of ninhydrin on the immune serum precipitants in horse].
Bulletin de la Societe de chimie biologique    January 1, 1953   Volume 35, Issue 10 1201-1207 
TAYEAU F, FAURE F.No abstract available
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