|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6
|
|
pubmed:dateCreated |
1999-1-15
|
|
pubmed:abstractText |
The 28 kDa secretory protein is one of the abundant water-soluble proteins in olfactory epithelium of mammals. Analysis of partial amino acid sequence of the 28 kDa protein strongly suggested that it belongs to a new family of highly conserved antioxidant proteins requiring thiol for their antioxidant activity (TSA/AhpC family). In the present study, we found the 28 kDa protein to have thiol-dependent antioxidant activity, thereby protecting radical-sensitive proteins such as glutamine synthetase and hemoglobin from oxidative modification caused by thiol-dependent metal ion-catalyzed oxidation system. The purified 28 kDa protein did not possess catalase or glutathione peroxidase activities, and required thiols to exhibit its antioxidant activity. The 28 kDa protein is the first member of the family of thiol-specific antioxidants identified in olfactory epithelium and the first secretory protein shown to be thiol-specific antioxidant.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Fenton's reagent,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate-Ammonia Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxiredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0891-5849
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
25
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
654-9
|
|
pubmed:dateRevised |
2007-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:9801064-Animals,
pubmed-meshheading:9801064-Antioxidants,
pubmed-meshheading:9801064-Glutamate-Ammonia Ligase,
pubmed-meshheading:9801064-Hemoglobins,
pubmed-meshheading:9801064-Hydrogen Peroxide,
pubmed-meshheading:9801064-Iron,
pubmed-meshheading:9801064-Neoplasm Proteins,
pubmed-meshheading:9801064-Olfactory Mucosa,
pubmed-meshheading:9801064-Oxidative Stress,
pubmed-meshheading:9801064-Peroxidases,
pubmed-meshheading:9801064-Peroxiredoxins,
pubmed-meshheading:9801064-Proteins,
pubmed-meshheading:9801064-Rats,
pubmed-meshheading:9801064-Reactive Oxygen Species,
pubmed-meshheading:9801064-Sulfhydryl Compounds
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
Identification of a 28 kDa secretory protein from rat olfactory epithelium as a thiol-specific antioxidant.
|
|
pubmed:affiliation |
Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region. peshenko@venus.iteb.serpukhov.su
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
