| pubmed-article:3118867 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3118867 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:3118867 | lifeskim:mentions | umls-concept:C0056097 | lld:lifeskim |
| pubmed-article:3118867 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:3118867 | lifeskim:mentions | umls-concept:C0037378 | lld:lifeskim |
| pubmed-article:3118867 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:3118867 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:3118867 | lifeskim:mentions | umls-concept:C0998121 | lld:lifeskim |
| pubmed-article:3118867 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3118867 | pubmed:dateCreated | 1987-11-27 | lld:pubmed |
| pubmed-article:3118867 | pubmed:abstractText | The cold agglutinin isolated from the albumin gland of the snail Achatina fulica was modified with various chemical reagents in order to detect the amino acids and/or carbohydrate residues present in its carbohydrate-binding sites. Treatment with reagents considered specific for modification of lysine, arginine and tryptophan residues of the cold agglutinin did not affect the carbohydrate-binding activity of the agglutinin. Modification of tyrosine residues showed some change. However, modification with carbodiimide followed by alpha-aminobutyric acid methyl ester causes almost complete loss of its binding activity, indicating the involvement of aspartic acid and glutamic acid in its carbohydrate-binding activity. The carbohydrate residues of the cold agglutinin were removed by beta-elimination reaction, indicating that the sugars are O-glycosidically linked to protein part of the molecule. Removal of galactose residues from the cold agglutinin by the action of beta-galactosidase indicated that the galactose molecules are beta-linked. These carbohydrate-modified glycoproteins showed a marked change in agglutination property, i.e. they agglutinated rabbit erythrocytes at both 10 degrees C and 25 degrees C, indicating that the galactose residues of the glycoprotein play an important role in the cold-agglutination property of the glycoprotein. The c.d. data showed the presence of an almost identical type of random-coil conformation in the native cold agglutinin at 10 degrees C and in the carbohydrate-modified glycoprotein at 10 degrees C and 25 degrees C. This particular random-coil conformation is essential for carbohydrate-binding property of the agglutinin. | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3118867 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3118867 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3118867 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3118867 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:3118867 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3118867 | pubmed:author | pubmed-author:SenA KAK | lld:pubmed |
| pubmed-article:3118867 | pubmed:author | pubmed-author:SarkarMM | lld:pubmed |
| pubmed-article:3118867 | pubmed:author | pubmed-author:MitreHH | lld:pubmed |
| pubmed-article:3118867 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3118867 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3118867 | pubmed:volume | 246 | lld:pubmed |
| pubmed-article:3118867 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3118867 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3118867 | pubmed:pagination | 157-61 | lld:pubmed |
| pubmed-article:3118867 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:meshHeading | pubmed-meshheading:3118867-... | lld:pubmed |
| pubmed-article:3118867 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3118867 | pubmed:articleTitle | Studies on chemical modification of cold agglutinin from the snail Achatina fulica. | lld:pubmed |
| pubmed-article:3118867 | pubmed:affiliation | Indian Institute of Chemical Biology, Jadavpur, Calcutta, India. | lld:pubmed |
| pubmed-article:3118867 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3118867 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3118867 | lld:pubmed |
