Source:http://linkedlifedata.com/resource/pubmed/id/10082950
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-5-6
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pubmed:abstractText |
A cDNA coding for plaice (Pleuronectes platessa) alpha1-microglobulin (Leaver et al., 1994, Comp. Biochem. Physiol. 108B, 275-281) was expressed and purified from baculovirus-infected insect cells. Specific monoclonal antibodies were then prepared and used to isolate the protein from plaice liver and serum. Mature 28.5 kDa alpha1-microglobulin was found in both liver and serum. The protein consisted of an 184 amino acid peptide with a complex N-glycan in position Asn123, one intrachain disulfide bridge and a yellow-brown chromophore. Physicochemical characterization indicated a globular shape with a frictional ratio of 1.37, electrophoretic charge-heterogeneity and antiparallel beta-sheet structure. A smaller, incompletely glycosylated, yellow-brown alpha1-microglobulin as well as a 45 kDa precursor protein were also found in liver. The chromophore was found to be linked to alpha1-microglobulin intracellularly. Recombinant plaice alpha1-microglobulin isolated from insect cells had the same N-terminal sequence, globular shape and yellow-brown color as mature alpha1-microglobulin, but carried a smaller, fucosylated, non-sialylated N-glycan in the Asn123 position. The concentration of alpha1-microglobulin in plaice serum was 20 mg/l and it was found both as a 28.5 kDa component and as high molecular weight components. Thus, the size, shape, charge and color of plaice alpha1-microglobulin were similar to mammalian alpha1-microglobulin, indicating a high degree of structural conservation between fish and human alpha1-microglobulin. The monoclonal antibodies against plaice alpha1-microglobulin cross-reacted with human alpha1-microglobulin, emphasizing the structural similarity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
1430
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
222-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10082950-Alpha-Globulins,
pubmed-meshheading:10082950-Animals,
pubmed-meshheading:10082950-Antibodies, Monoclonal,
pubmed-meshheading:10082950-Baculoviridae,
pubmed-meshheading:10082950-Cell Line,
pubmed-meshheading:10082950-Cross Reactions,
pubmed-meshheading:10082950-DNA, Complementary,
pubmed-meshheading:10082950-Flounder,
pubmed-meshheading:10082950-Liver,
pubmed-meshheading:10082950-Molecular Structure
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pubmed:year |
1999
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pubmed:articleTitle |
Isolation of plaice (Pleuronectes platessa) alpha1-microglobulin: conservation of structure and chromophore.
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pubmed:affiliation |
Section for Molecular Signaling, Department of Cell and Molecular Biology, Lund University, P.O. Box 94, S-221 00, Lund, Sweden.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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