| pubmed-article:54922 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:54922 | lifeskim:mentions | umls-concept:C0019628 | lld:lifeskim |
| pubmed-article:54922 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
| pubmed-article:54922 | lifeskim:mentions | umls-concept:C0162326 | lld:lifeskim |
| pubmed-article:54922 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:54922 | lifeskim:mentions | umls-concept:C0728938 | lld:lifeskim |
| pubmed-article:54922 | lifeskim:mentions | umls-concept:C0002131 | lld:lifeskim |
| pubmed-article:54922 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:54922 | pubmed:dateCreated | 1976-4-2 | lld:pubmed |
| pubmed-article:54922 | pubmed:abstractText | Techniques for the amino acid sequence analysis of subnanomole quantities of polypeptides have been applied to characterize beta2-microglobulin and transplantation antigens of the mouse isolated from spleen cells by indirect immunoprecipitation. Eleven residues were identified throughout the NH2-terminal 27 residues of the beta2-microglobulin; all were identical to residues seen at the corresponding positions of beta2-microglobulins from other species. Two K and two D transplantation antigens were examined and the following generalizations emerged from the limited partial amino-acid sequence data: (1) the K and D molecules are homologous to one another; (2) they do not show amino acid sequence homology with immunoglobulins; (3) the two K and two D molecules differ from one another by multiple amino acid substitutions; and (4) the K molecules as a class cannot be distinguished from the D molecules as a class. The genetic and evolutionary implications of these observations are discussed. | lld:pubmed |
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| pubmed-article:54922 | pubmed:language | eng | lld:pubmed |
| pubmed-article:54922 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:54922 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:54922 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:54922 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:54922 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:54922 | pubmed:author | pubmed-author:HoodLL | lld:pubmed |
| pubmed-article:54922 | pubmed:author | pubmed-author:SilverJJ | lld:pubmed |
| pubmed-article:54922 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:54922 | pubmed:volume | 73 | lld:pubmed |
| pubmed-article:54922 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:54922 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:54922 | pubmed:pagination | 599-603 | lld:pubmed |
| pubmed-article:54922 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:54922 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:54922 | pubmed:articleTitle | Structure and evolution of transplantation antigens: partial amino-acid sequences of H-2K and H-2D alloantigens. | lld:pubmed |
| pubmed-article:54922 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:54922 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:54922 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:54922 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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