| pubmed-article:12387870 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12387870 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12387870 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:12387870 | lifeskim:mentions | umls-concept:C1097060 | lld:lifeskim |
| pubmed-article:12387870 | pubmed:issue | 1-3 | lld:pubmed |
| pubmed-article:12387870 | pubmed:dateCreated | 2002-10-21 | lld:pubmed |
| pubmed-article:12387870 | pubmed:abstractText | Spermatid-specific thioredoxin-1 (Sptrx-1) is the first member of the thioredoxin family of proteins with a tissue-specific expression pattern, found exclusively in the tail of elongating spermatids and spermatozoa. We describe here further biochemical characterization of human Sptrx-1 protein structure and enzymatic activity. In gel filtration chromatography human Sptrx-1 eluates as a 400 kDa protein consistent with either an oligomeric form, not maintained by intermolecular disulfide bonding, and/or a highly asymmetrical structure. Analysis of circular dichroism spectra of fragments 1-360 and 361-469 and comparison to spectra of full-length Sptrx-1 supports a two-domain organization with a largely unstructured N-terminal domain and a folded thioredoxin-like C-terminal domain. Functionally, Sptrx-1 behaves as an oxidant in vitro when using selenite, but not oxidized glutathione, as electron acceptor. This oxidizing enzymatic activity suggests that Sptrx-1 might govern the stabilization (by disulfide cross-linking) of the different structures in the developing tail of spermatids and spermatozoa. | lld:pubmed |
| pubmed-article:12387870 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12387870 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12387870 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12387870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12387870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12387870 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12387870 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12387870 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12387870 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:CuiX SXS | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:KieselbachTho... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:HolmgrenArneA | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:GustafssonJan... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:Miranda-Vizue... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:LadensteinRud... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:BerndtKurt... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:JohanssonCatr... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:JiménezAlbert... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:LjungJohannaJ | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:SagemarkJohan... | lld:pubmed |
| pubmed-article:12387870 | pubmed:author | pubmed-author:TibbelinGudru... | lld:pubmed |
| pubmed-article:12387870 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12387870 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:12387870 | pubmed:volume | 530 | lld:pubmed |
| pubmed-article:12387870 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12387870 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12387870 | pubmed:pagination | 79-84 | lld:pubmed |
| pubmed-article:12387870 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:meshHeading | pubmed-meshheading:12387870... | lld:pubmed |
| pubmed-article:12387870 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12387870 | pubmed:articleTitle | Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity. | lld:pubmed |
| pubmed-article:12387870 | pubmed:affiliation | Center for Biotechnology, Department of Biosciences at NOVUM, Karolinska Institutet, S-14157 Huddinge, Sweden. | lld:pubmed |
| pubmed-article:12387870 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12387870 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:84203 | entrezgene:pubmed | pubmed-article:12387870 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:12387870 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:12387870 | lld:entrezgene |
