The stoichiometry of J chain in human secretory dimeric IgA
Dimeric human secretory IgA was completely reduced with mercaptoethanol and alkylated with [ 14C] iodoacetamide. The component polypeptide chains were separated by high performance gel filtration in 5 M guanidine HCl into two fractions: one containing secretory component (SC) + heavy (H) chains; and...
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| Veröffentlicht in: | Molecular immunology 1986-05, Vol.23 (5), p.541-544 |
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| container_title | Molecular immunology |
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| creator | Zikan, J. Mestecky, J. Kulhavy, R. Bennett, J.C. |
| description | Dimeric human secretory IgA was completely reduced with mercaptoethanol and alkylated with [
14C] iodoacetamide. The component polypeptide chains were separated by high performance gel filtration in 5
M guanidine HCl into two fractions: one containing secretory component (SC) + heavy (H) chains; and the second containing light (L) + J chains. L and J chains were subsequently separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS) or in alkaline urea. Calculations of the J chain stoichiometry in the dimeric secretory IgA (S-IgA) molecule were based on: (1) the measurement of the ratio of radioactivities of SC + H chain and L + J chain-fractions or L chain-and J chain-fractions; (2) the known stoichiometry of SC, H and L chains; and (3) the known number of half-cystine residues in the component polypeptide chains of S-IgA molecule. The data demonstrated that one molecule of dimeric S-IgA contains approx. one J chain. |
| doi_str_mv | 10.1016/0161-5890(86)90117-3 |
| format | Article |
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14C] iodoacetamide. The component polypeptide chains were separated by high performance gel filtration in 5
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14C] iodoacetamide. The component polypeptide chains were separated by high performance gel filtration in 5
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14C] iodoacetamide. The component polypeptide chains were separated by high performance gel filtration in 5
M guanidine HCl into two fractions: one containing secretory component (SC) + heavy (H) chains; and the second containing light (L) + J chains. L and J chains were subsequently separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS) or in alkaline urea. Calculations of the J chain stoichiometry in the dimeric secretory IgA (S-IgA) molecule were based on: (1) the measurement of the ratio of radioactivities of SC + H chain and L + J chain-fractions or L chain-and J chain-fractions; (2) the known stoichiometry of SC, H and L chains; and (3) the known number of half-cystine residues in the component polypeptide chains of S-IgA molecule. The data demonstrated that one molecule of dimeric S-IgA contains approx. one J chain.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>3092031</pmid><doi>10.1016/0161-5890(86)90117-3</doi><tpages>4</tpages></addata></record> |
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| ispartof | Molecular immunology, 1986-05, Vol.23 (5), p.541-544 |
| issn | 0161-5890 1872-9142 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Chemical Phenomena Chemistry Chromatography, Gel Electrophoresis, Polyacrylamide Gel Humans Immunoglobulin A, Secretory Immunoglobulin J-Chains |
| title | The stoichiometry of J chain in human secretory dimeric IgA |
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