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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-10-28
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pubmed:abstractText |
Cobalamin-binding protein has been purified from chicken egg yolk by using DEAE-cellulose with a NaCl gradient. The resultant protein fraction was subjected to bioaffinity chromatography. The Mr was 38,000 by SDS-PAGE and 39,000 by gel filtration, and indicated that it was a glycoprotein. The Stokes radius was 4.3 nm and the pI 4.1. The protein bound 57CO.B12 with a molar ratio of 1:1 and a Kd of 0.41 microM. The CBP composed 296 amino acids residues. The protein-ligand interaction was inhibited by Cbl analogues.
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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 |
Sep
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
998
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
102-4
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:2790050-Amino Acids,
pubmed-meshheading:2790050-Animals,
pubmed-meshheading:2790050-Chick Embryo,
pubmed-meshheading:2790050-Chromatography, Affinity,
pubmed-meshheading:2790050-Chromatography, DEAE-Cellulose,
pubmed-meshheading:2790050-Chromatography, Gel,
pubmed-meshheading:2790050-Egg Yolk,
pubmed-meshheading:2790050-Glycoproteins,
pubmed-meshheading:2790050-Transcobalamins
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pubmed:year |
1989
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pubmed:articleTitle |
Purification and partial characterization of a cobalamin-binding protein from chicken egg yolk.
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pubmed:affiliation |
Department of Animal Biochemistry, Jagiellonian University, Kraków, Poland.
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pubmed:publicationType |
Journal Article
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