| pubmed-article:3977821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C0441833 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C0020835 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C0456378 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C0205257 | lld:lifeskim |
| pubmed-article:3977821 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:3977821 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3977821 | pubmed:dateCreated | 1985-4-8 | lld:pubmed |
| pubmed-article:3977821 | pubmed:abstractText | The BALB/c IgA (immunoglobulin A) myeloma protein M167 contained on average 5.7 free SH groups per IgA dimer. These groups were preponderantly on the heavy chains and comprised two distinct populations: 3.3 exposed SH groups per dimer in the Fc region, and 2.4 buried SH groups per dimer in the Fd region, detectable o only after denaturation. To locate the cysteine residues involved, labelled peptides were purified from thermolysin digests of radioalkylated IgA by high-performance liquid chromatography. From the amino acid compositions of the peptides, the exposed thiol groups were assigned to Cys-307 in the C alpha 2 domain, which thus existed in the reduced form to an extent exceeding 80%. This residue may allow attachment of secretory component to dimer IgA in the mouse to proceed via thiol-disulphide exchange. The buried thiol groups were assigned to Cys-150 and Cys-208, in the C alpha 1 domain, each being in the reduced form to the extent of approx. 30%. This pair of residues would normally give rise to the characteristic intradomain disulphide bridge. It appears that disulphide formation is not a crucial event during folding of the C alpha 1 domain in IgA biosynthesis. The sequence in the region 140-151 was re-investigated, and residue 142 was shown to be serine, not cysteine, helping explain the lack of heavy-chain-light chain bonding in BALB/c mouse IgA. A disulphide-bond model for mouse IgA is proposed on the basis of these assignments and other features of the mouse alpha-chain sequence. | lld:pubmed |
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| pubmed-article:3977821 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3977821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3977821 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3977821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3977821 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3977821 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3977821 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3977821 | pubmed:author | pubmed-author:YoungN MNM | lld:pubmed |
| pubmed-article:3977821 | pubmed:author | pubmed-author:CockleS ASA | lld:pubmed |
| pubmed-article:3977821 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3977821 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3977821 | pubmed:volume | 225 | lld:pubmed |
| pubmed-article:3977821 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3977821 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3977821 | pubmed:pagination | 113-25 | lld:pubmed |
| pubmed-article:3977821 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3977821 | pubmed:meshHeading | pubmed-meshheading:3977821-... | lld:pubmed |
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| pubmed-article:3977821 | pubmed:meshHeading | pubmed-meshheading:3977821-... | lld:pubmed |
| pubmed-article:3977821 | pubmed:meshHeading | pubmed-meshheading:3977821-... | lld:pubmed |
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| pubmed-article:3977821 | pubmed:meshHeading | pubmed-meshheading:3977821-... | lld:pubmed |
| pubmed-article:3977821 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:3977821 | pubmed:articleTitle | The thiol groups of mouse immunoglobulin A. Incomplete formation of the C alpha 1-domain disulphide bridge. | lld:pubmed |
