| pubmed-article:2363694 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2363694 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:2363694 | lifeskim:mentions | umls-concept:C0055966 | lld:lifeskim |
| pubmed-article:2363694 | lifeskim:mentions | umls-concept:C0036825 | lld:lifeskim |
| pubmed-article:2363694 | lifeskim:mentions | umls-concept:C1415188 | lld:lifeskim |
| pubmed-article:2363694 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:2363694 | lifeskim:mentions | umls-concept:C0204514 | lld:lifeskim |
| pubmed-article:2363694 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2363694 | pubmed:dateCreated | 1990-8-8 | lld:pubmed |
| pubmed-article:2363694 | pubmed:abstractText | Sulphated glycoprotein 2 (SGP-2) is the major secreted protein product of rat Sertoli cells; likewise, clusterin is a major constituent of ram rete testis fluid. Isolation and sequencing of the intact subunits and peptides derived from clusterin show that it is the ram homologue of rat SGP-2. Human serum protein 40,40 (SP-40,40), a component of the SC5b-9 complex of complement, has recently been reported to be the human homologue of rat SGP-2. Analysis of the amino acid sequences of rat SGP-2 and human SP-40,40 show that both of these proteins have a significant relationship to the heavy chain of myosin. The regions of highest sequence similarity correspond to the major amphipathic domains in SGP-2/SP-40,40 and the long alpha-helical-tail domain of myosin, which forms a rod-like structure. SGP-2 has anomalous sedimentation behaviour which indicates that it probably exists in an extended conformation. A putative dinucleotide-binding structure has been identified in the longest stretch of identity between SGP-2 and SP-40,40. Elucidation of these features of SGP-2 and SP-40,40 may help to direct future studies into the role of these proteins in the reproductive and complement systems. | lld:pubmed |
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| pubmed-article:2363694 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2363694 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2363694 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2363694 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2363694 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2363694 | pubmed:author | pubmed-author:WongKK | lld:pubmed |
| pubmed-article:2363694 | pubmed:author | pubmed-author:FritzI BIB | lld:pubmed |
| pubmed-article:2363694 | pubmed:author | pubmed-author:GriswoldM DMD | lld:pubmed |
| pubmed-article:2363694 | pubmed:author | pubmed-author:TsurutaJ KJK | lld:pubmed |
| pubmed-article:2363694 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2363694 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2363694 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:2363694 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2363694 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2363694 | pubmed:pagination | 571-8 | lld:pubmed |
| pubmed-article:2363694 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2363694 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2363694 | pubmed:articleTitle | Structural analysis of sulphated glycoprotein 2 from amino acid sequence. Relationship to clusterin and serum protein 40,40. | lld:pubmed |
| pubmed-article:2363694 | pubmed:affiliation | Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660. | lld:pubmed |
| pubmed-article:2363694 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2363694 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2363694 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2363694 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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