Binding specificities of the lectins PNA, WGA and UEA I to polyvinylchloride-adsorbed glycosphingolipids
The binding specificities of the lectins PNA (peanut agglutinin), WGA (wheat germ agglutinin), and UEA I ( Ulex europeus agglutinin I) against glycosphingolipids were investigated using an enzyme-linked immunosorbent assay (ELISA), utilizing the biotin-avidin system for detection of bound lectin. PN...
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Published in | FEBS letters Vol. 205; no. 1; pp. 51 - 55 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
01.09.1986
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | The binding specificities of the lectins PNA (peanut agglutinin), WGA (wheat germ agglutinin), and UEA I (
Ulex europeus agglutinin I) against glycosphingolipids were investigated using an enzyme-linked immunosorbent assay (ELISA), utilizing the biotin-avidin system for detection of bound lectin. PNA showed the highest affinity to GA1, but also bound, though less strongly, to GM1 and GD1b. WGA bound to 3'-nLM1 and 6'-nLM1, the former twice as strongly as the latter, but not to any sialic acid containing glycolipid of the gangliotetraose series. UEA I showed a high affinity for the Le
a glycolipid which has an α 1-4 linked fucose but not for the glycolipids with αl-3 or α 1–2 linked fucose. Interestingly, 3'-nLM1 and nLA1, glycolipids lacking fucose, also bound UEA I. The results show that lectins should be used with caution for establishing terminal sugar sequences in glycosphingolipids. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(86)80864-X |