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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-7-1
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pubmed:abstractText |
Molecules containing the 33-kDa plasma protein alpha1-microglobulin were isolated from human plasma by anti-(alpha1-microglobulin) affinity chromatography. Five major bands could be seen after electrophoretic separation of the alpha1-microglobulin-containing proteins under native conditions. Immunoblotting demonstrated alpha1-microglobulin in all five bands. Two of these have been described previously: free alpha1-microglobulin and alpha1-microglobulin complexed with IgA (IgA x alpha1-microglobulin). The other three bands were identified as prothrombin alpha1-microglobulin, albumin x alpha1-microglobulin and dimeric alpha1-microglobulin. Prothrombin x alpha1-microglobulin were 1:2 and 1:1 complexes which carried approximately 1% of total alpha1-microglobulin, had molecular masses of about 145 kDa and 110 kDa upon SDS/PAGE and dissociated completely to free alpha1-microglobulin and prothrombin (72 kDa) when reducing agents were added, suggesting that the complexes were stabilized by disulfide bonds. The alpha1-microglobulin molecules did not inhibit cleavage of prothrombin by factor Xa and were bound to the peptides which were released upon activation of prothrombin. Albumin x alpha1-microglobulin, corresponding to 7% of total plasma alpha1-microglobulin, was a mixture between 1:1 and 1:2 complexes, with masses upon SDS/PAGE of approximately 100 kDa and 135 kDa, respectively. Both these complexes dissociated only partially to free alpha1-microglobulin and albumin when reducing agents were added. The albumin x alpha1-microglobulin complexes carried a yellow-brown chromophore similar to free alpha1-microglobulin. The complex-binding to alpha1-microglobulin did not block the fatty-acid-binding ability of albumin. The plasma concentrations of albumin x alpha1-microglobulin and prothrombin x alpha1-microglobulin were estimated to 5.2 mg/l and 1.1 mg/l, respectively.
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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/Alpha-Globulins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin A,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Prothrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-1-microglobulin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
245
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
676-83
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:9183005-Alpha-Globulins,
pubmed-meshheading:9183005-Humans,
pubmed-meshheading:9183005-Immunoglobulin A,
pubmed-meshheading:9183005-Macromolecular Substances,
pubmed-meshheading:9183005-Protein Binding,
pubmed-meshheading:9183005-Prothrombin,
pubmed-meshheading:9183005-Serum Albumin
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pubmed:year |
1997
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pubmed:articleTitle |
Prothrombin, albumin and immunoglobulin A form covalent complexes with alpha1-microglobulin in human plasma.
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pubmed:affiliation |
The Section for Molecular Signalling, Department of Cell and Molecular Biology, Lund University, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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