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At least 19 recordsLinked to original sources
PubMed1977

[Secretory immunoglobulin A].

Secretory IgA is the prevailung immunoglobulin on the mucous membranes of different tissues. It is a polymer immunoglobulin and in comparison to the serum IgA the secretory IgA has a additional polypeptide chain, the secretory component. The secretory IgA is synthesized locally in the mucosa. Secretory IgA is a very important factor in the immune defence of the mucous membranes. Secretory antibodies are regulated independently from serum antibodies. They show a virus neutralizing effect and activities against bacteria and lifeless noxa. The mechanism is not yet clear. It is possible, that the reaction of the secretory IgA with the antigen prevents settlement of microorganisms on the mucous membranes. The clinical importance of secretory IgA is undoubted especially the deference of the mucosa in cases of a virus infection.

Antibodies↗
PubMed1977

Isolation and characterization of canine secretory immunoglobulin M.

Canine secretory immunoglobulin M, isolated from both colostrum and bronchial secretions, contained the unique glycoprotein bound secretory component. The presence of this extra subunit accounted for the differences in size, quaternary structure, and antigenicity observed upon comparison of secretory immunoglobulin M with its serum counterpart. Approximately 90% of the isolated secretory immunoglobulin M contained covalently bound secretory component while, in the remainder of the population, secretory component was loosely attached and easily dissociated from the immunoglobulin. Following peptide bond cleavage with cyanogen bromide, the release of bound secretory component and J chain from secretory immunoglobulin M was not detected. Because cyanogen bromide cleavage of secretory immunoglobulin A results in the release of these subunits, differences in the primary structure of secretory immunoglobulin M and secretory immunoglobulin A must exist around the binding sites for secretory component and J chain.

Animals↗
PubMed1975

[Study of human secretory immunoglobulin A. I. Obtaining monospecific antiserum to human secretory immunoglobulin A].

A method of obtaining monospecific antiserum to the human secretory IgA is described. Immunochemically pure secretory IgA (isolated from human colostrum by fractionation with ammonium sulfate and gel-filtration on Sephadex G-200) was used for immunization of rabbits or sheep. Heterologous antibodies were removed by adsorption with commercial gamma globulin, normal serum, the serum of a patient suffering from A-myeloma with the IgA polymere and purified lactoferrin. Monospecific antiserum to the secretory IgA gave a reaction of complete immunological identity with the secretory IgA and a free secretory component.

Adsorption↗
PubMed1978

[Method of preparation and evaluation of antisera for the differential determination of secretory immunoglobulin A and free secretory component in biological fluids].

One of the pressing tasks in the study of local nonsusceptibility to infectious diseases and immunochemical analysis of the external secretion is recording of the level of various forms of the secretory IgA (SIgA) and of the secretory component (SC) in various biological fluids. Indication and measurment of the concentrations of the mentioned proteins encounter serious difficulties caused by heterogeneity of their molecular forms. It was shown that the antisera to the whole molecule of SIgA and SC are of no use. On the basis of a new method of purification of free SC and technology of preparation of monospecific antisera capable of separation of SIgA and free SC there were obtained diagnostic antisera for the quantitative recording and differentiation of various forms of IgA and SC in biological fluids. A reliable measurement of the SIgA and SC concentration in some external secretion was carried out with the aid of the mentioned preparations without any complicated chromatographic experiments.

Animals↗
PubMed1978

Secretory immunoglobulin A and G antibodies prevent adhesion of Escherichia coli to human urinary tract epithelial cells.

The adhesion of Escherichia coli to human urinary tract epithelial cells was inhibited by commercial gamma globulin, the total immunoglobulin fraction of human breast milk and urine, as well as the isolated immunoglobulin G and secretory immunoglobulin A fractions of urine from patients with acute pyelonephritis. Urinary anti-O6 antibodies reduced the adhesion of several O6 strains. Absorption of antibodies to the lipopolysaccharide of the adhering strain markedly decreased the antiadhesive capacity of all the immunoglobulin preparations, whereas elimination of antibodies to the capsular polysaccharide antigen consistently had a small but not significant effect. When urine was absorbed with whole, live bacteria of the patients' infecting strains, the antiadhesive effect completely disappeared. Absorption with bacteria lacking pili only partially reduced this effect.

Antibodies, Bacterial↗
PubMed1979

Effect of a disulfide-interchange enzyme on the assembly of human secretory immunoglobulin A from immunoglobulin A and free secretory component.

A disulfide-interchange enzyme from rat liver microsomes was found to promote binding in vitro of human free secretory component (SC) to dimeric serum-type IgA containing J chain, as assessed by immune precipitation and gel filtration. This effect was greater withe native than with partially reduced SC. Most of the bound SC was covalently linked, as determined by electrophoresis in polyacrylamide gels in detergent. The enzyme did not promote binding of native or partially reduce SC to IgG, IgA monomer, IgA dimer without J chain, or IgM. In the case of IgM, the enzyme did, however, promote covalent bonding of previously non-covalently linked SC. The results overall suggest that a disulfide-interchange enzyme could play a role in vivo in the cell-associated assembly of secretory IgA by promoting the covalent attachment of SC to a dimer of serum-type IgA and that the J chain in the IgA dimer contributes to the enzyme effect.

Animals↗
PubMed1977

Chicken secretory immunoglobulin: chemical and immunological characterization of chicken IgA.

1. Chicken IgA purified from biliary fluids was chemically and immunologically characterized. 2. Chicken IgA was determined to be the only immunoglobulin class present in bile. Gel filtration studies reveal polymeric IgA e.g. 17-19S. 3. Antigenically, chicken IgA is distinct from chicken IgG, and IgM. 4. Chicken IgA does not show antigenic homology to human IgA. 5. SDS poly-acrylamide gel electrophoresis revealed IgA to possess heavy chains of 60,000 and light chains of 24,000 mol. wt, respectively. 6. Peptide mapping of tryptic digests of chicken alpha chains reveals approximately 35 peptides. The peptide map pattern is distinct from chicken gamma chains.

Animals↗
PubMed1978

Combined therapy of human interferon (HI) and secretory immunoglobulin (S-IgA) in the treatment of human herpetic keratitis.

The topical action of a combined therapy of human interferon (3000 U/ml) and secretory immunoglobulin IgA (1,5 mg/ml) was studied in 56 patients with herpetic keratitis. The pain and photophobia disappeared within 48 h after the beginning of treatment and a marked reduction of the corneal lesion during the first week of treatment was observed in all the patients. The therapy was effective, with complete healing of the lesion in 94.8% of cases; 72.2% of them healed in less than 15 days. The highest frequency of healing was between 5 and 10 days, and the rest up to 30 days. Humoral, immunological and delayed hypersensitivity studies were carried out in 36 patients.

Adolescent↗
PubMed1979

[Morphological and immuno-cytological classification of secretory immunoglobulin producing malignant lymphomas (author's transl)].

After an introduction about the frequency of "secretory" immunoglobulin producing malignant lymphomas and the histological equivalent of intracytoplasmatic immunoglobulin the results of a co-operative retrospective study on 102 cases of immunocytoma and 28 cases of immunoblastoma are discussed. According to the different types of physiological plasma cell reaction lymphoplasmacytoid immunocytoma might be functionally interpreted as "parafollicular" immunocytoma, whereas lymphoplasmacytic and polymorphous immunocytoma might be functionally considered as a "transfollicular" one. These subtypes of the immunocytoma show differences in morphology, immunocytology, primary localization and occurrence of leukemia.

Humans↗
PubMed1977

The subunit and polypeptide-chain structure of rabbit secretory immunoglobulin A. Isolation of a proteolytic fragment suitable for sequence studies on the variable region of alpha-chain.

A method was developed for the preparation of a proteolytic fragment of rabbit secretory immunoglobulin A (sIgA) which contains the variable region of the alpha-chain; this fragment is suitable for primary-sequence studies. The serologically defined subclasses of sIgA are shown to correlate partially with the nature of the binding of a constituent chain of sIgA, called secretory piece. Data are also presented on the relative resistance of sIgA to enzymic and reductive cleavage, compared with immunoglobulin G.

Amino Acids↗