Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1995-10-4
|
pubmed:abstractText |
We report that alpha-2-macroglobulin (alpha 2M) can form complexes with a high molecular weight porcine mannan-binding protein (pMBP-28). The alpha 2M/pMBP-28 complexes was isolated by PEG-precipitation and affinity chromatography on mannan-Sepharose, protein A-Sepharose and anti-IgM Sepharose. The occurrence of alpha 2M/pMBP-28 complexes was further indicated by crossed immunoelectrophoresis and by use of an anti-alpha 2M affinity column and chelating Sepharose loaded with Zn2+. The eluates from these affinity columns showed alpha 2M subunits (94 and 180 kDa) and pMBP subunits (28kDa) in SDS-PAGE, which reacted with antibodies against alpha 2M and pMBP-28, respectively, in Western blotting. Furthermore, alpha 2M/pMBP-28 complexes were demonstrated by electron microscopy. Fractionation of pMBP-containing D-mannose eluate from mannan-Sepharose on Superose 6 showed two protein peaks which reacted with anti-C1 s antibodies in ELISA, one of about 650-800 kDa, which in addition contained pMBP-28 and anti-alpha 2M reactive material, the other with an M(r) of 100-150 kDa. The latter peak revealed rhomboid molecules (7 x 15 nm) in the electron microscope and a 67 kDa band in SDS-PAGE under reducing conditions. This band was also seen in eluates from the anti-alpha 2M and chelating Sepharose columns. Based on these observations and previous findings by other investigators of a serine protease with about 67 kDa subunits which copurifies with human MBP we propose a model for the interaction of pMBP-28 with alpha 2M.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Collagenases,
http://linkedlifedata.com/resource/pubmed/chemical/Collectins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Macroglobulins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0300-9475
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
42
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
373-80
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7544912-Animals,
pubmed-meshheading:7544912-Blotting, Western,
pubmed-meshheading:7544912-Carrier Proteins,
pubmed-meshheading:7544912-Chelating Agents,
pubmed-meshheading:7544912-Chromatography, Affinity,
pubmed-meshheading:7544912-Chromatography, Gel,
pubmed-meshheading:7544912-Collagenases,
pubmed-meshheading:7544912-Collectins,
pubmed-meshheading:7544912-Immunoelectrophoresis, Two-Dimensional,
pubmed-meshheading:7544912-Microscopy, Electron,
pubmed-meshheading:7544912-Protein Binding,
pubmed-meshheading:7544912-Swine,
pubmed-meshheading:7544912-alpha-Macroglobulins
|
pubmed:year |
1995
|
pubmed:articleTitle |
Mannan-binding protein forms complexes with alpha-2-macroglobulin. A protein model for the interaction.
|
pubmed:affiliation |
Department of Medical Microbiology, Odense University, Denmark.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|