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Título: | Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity |
Autor: | Jiménez, Alberto CSIC ORCID CVN; Johansson, Catrine; Ljung, Johanna; Sagemark, Johan; Berndt, Kurt D.; Ren, Bin; Tibbelin, Gudrun; Ladenstein, Rudolf; Kieselbach, Thomas; Holmgren, Arne; Gustafsson, Jan-Åke; Miranda-Vizuete, Antonio CSIC ORCID | Palabras clave: | Thioredoxin Spermatozoon Fibrous sheath Redox regulation |
Fecha de publicación: | 26-sep-2002 | Editor: | Elsevier | Citación: | FEBS Letters 530(1-3): 79-84 (2002) | Resumen: | 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. | Descripción: | 24 páginas, 5 figuras. | Versión del editor: | http://dx.doi.org/10.1016/S0014-5793(02)03417-8 | URI: | http://hdl.handle.net/10261/47334 | DOI: | 10.1016/S0014-5793(02)03417-8 | ISSN: | 0014-5793 | E-ISSN: | 1873-3468 |
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