| pubmed-article:9023547 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C0020852 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C1264633 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C0205296 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C0052492 | lld:lifeskim |
| pubmed-article:9023547 | lifeskim:mentions | umls-concept:C1136160 | lld:lifeskim |
| pubmed-article:9023547 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:9023547 | pubmed:dateCreated | 1997-4-17 | lld:pubmed |
| pubmed-article:9023547 | pubmed:abstractText | Plant and animal lectins bind and cross-link certain multiantennary oligosaccharides, glycopeptides, and glycoproteins. This can lead to the formation of homogeneous cross-linked complexes, which may differ in their stoichiometry depending on the nature of the sugar receptor involved. As a precisely defined ligand, we have employed bovine asialofetuin (ASF), a glycoprotein that possesses three asparagine-linked triantennary complex carbohydrate chains with terminal LacNAc residues. In the present study, we have compared the carbohydrate cross-linking properties of two Lac-specific plant lectins, an animal lectin and a naturally occurring Lac-binding polyclonal immunoglobulin G subfraction from human serum with the ligand. Quantitative precipitation studies of the Lac-specific plant lectins, Viscum album agglutinin and Ricinus communis agglutinin, and the Lac-specific 16 kDa dimeric galectin from chicken liver demonstrate that these lectins form specific, stoichiometric cross-linked complexes with ASF. At low concentrations of ASF, 1:9 ASF/lectin (monomer) complexes formed with both plant lectins and the chicken lectin. With increasing concentrations of ASF, 1:3 ASF/lectin (monomer) complexes formed with the lectins irrespective of their source or size. The naturally occurring polyclonal antibodies, however, revealed a different cross-linking behavior. They show the formation of 1:3 ASF/antibody (per Fab moiety) cross-linked complexes at all concentrations of ASF. These studies demonstrate that Lac-specific plant and animal lectins as well as the Lac-binding immunoglobulin subfraction from specific stoichiometric cross-linked complexes with ASF. These results are discussed in terms of the structure-function properties of multivalent lectins and antibodies. | lld:pubmed |
| pubmed-article:9023547 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9023547 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9023547 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9023547 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9023547 | pubmed:issn | 0959-6658 | lld:pubmed |
| pubmed-article:9023547 | pubmed:author | pubmed-author:GuptaDD | lld:pubmed |
| pubmed-article:9023547 | pubmed:author | pubmed-author:BrewerC FCF | lld:pubmed |
| pubmed-article:9023547 | pubmed:author | pubmed-author:DonnWW | lld:pubmed |
| pubmed-article:9023547 | pubmed:author | pubmed-author:GabiusH JHJ | lld:pubmed |
| pubmed-article:9023547 | pubmed:author | pubmed-author:KaltnerHH | lld:pubmed |
| pubmed-article:9023547 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9023547 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:9023547 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9023547 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9023547 | pubmed:pagination | 843-9 | lld:pubmed |
| pubmed-article:9023547 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:meshHeading | pubmed-meshheading:9023547-... | lld:pubmed |
| pubmed-article:9023547 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:9023547 | pubmed:articleTitle | Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural lactose-binding immunoglobulin G fraction from human serum with asialofetuin. | lld:pubmed |
| pubmed-article:9023547 | pubmed:affiliation | Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. | lld:pubmed |
| pubmed-article:9023547 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9023547 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9023547 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9023547 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9023547 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9023547 | lld:pubmed |
