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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
30
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pubmed:dateCreated |
1992-11-25
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pubmed:abstractText |
The proteasome (multicatalytic protease complex), a high molecular weight protein complex, has been purified from spinach leaves by successive chromatography on DEAE-cellulose, Bio-Gel A-1.5m, DEAE-TOYOPEARL 650C, and DEAE-5PW. The molecular mass was estimated to be 850 kDa by gel filtration. Polyacrylamide gel electrophoresis of the proteasome gave a single protein band under nondenaturing conditions and at least 10 bands in the range of 21-32 kDa in the presence of sodium dodecyl sulfate. By electron microscopy after negative staining with uranyl acetate, the proteasome from spinach appeared as symmetrical ring-shaped particles. The substrate specificity of proteasomes indicates that they contain at least three types of activity, namely, chymotrypsin-like, Staphylococcus aureus V8 protease-like, and trypsin-like activities. The former two activities were enhanced by poly-L-lysine or sodium dodecyl sulfate. Moreover, we examined the immunological reactivities of proteasomes from various eukaryotes. As a result, cross-immunoreactivities of some subunits were observed. These properties of the proteasome are similar to those of proteasomes isolated from various other eukaryotic sources.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Dodecyl Sulfate
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21678-84
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1400479-Amino Acid Sequence,
pubmed-meshheading:1400479-Blotting, Western,
pubmed-meshheading:1400479-Chromatography, Gel,
pubmed-meshheading:1400479-Chromatography, Ion Exchange,
pubmed-meshheading:1400479-Cysteine Endopeptidases,
pubmed-meshheading:1400479-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1400479-Hydrogen-Ion Concentration,
pubmed-meshheading:1400479-Microscopy, Electron,
pubmed-meshheading:1400479-Molecular Sequence Data,
pubmed-meshheading:1400479-Multienzyme Complexes,
pubmed-meshheading:1400479-Plants,
pubmed-meshheading:1400479-Proteasome Endopeptidase Complex,
pubmed-meshheading:1400479-Sodium Dodecyl Sulfate,
pubmed-meshheading:1400479-Substrate Specificity
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pubmed:year |
1992
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pubmed:articleTitle |
Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea.
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pubmed:affiliation |
Department of Agricultural Chemistry, Faculty of Horticulture, Chiba University, Japan.
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pubmed:publicationType |
Journal Article
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