Characterization of binding of Gal beta 4GlcNAc-specific lectins from Erythrina cristagalli and Erythrina corallodendron to glycosphinogolipids. Detection, isolation, and characterization of a novel glycosphinglipid of bovine buttermilk.-Reference-Cited by-同舟云学术

Characterization of binding of Gal beta 4GlcNAc-specific lectins from Erythrina cristagalli and Erythrina corallodendron to glycosphinogolipids. Detection, isolation, and characterization of a novel glycosphinglipid of bovine buttermilk.

Published:1994-03 Issue:11 Volume:269 Page:8554-8563
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Teneberg S.,Angström J.,Jovall P.A.,Karlsson K.A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

1. Purification and Properties of a d-Galactose/N-Acetyl-d- galactosamine-Specific Lectin from Erythrina cristagalli

2. Binding of simple carbohydrates and some N-acetyllactosamine-containing oligosaccharides to Erythrina cristagalli agglutinin as followed with a fluorescent indicator ligand

3. Immunochemical studies on the combining site of the d-galactose/N-acetyl-d-galactosamine specific lectin from Erythrina cristagalli seeds

4. The glycolipid specificity ofErythrina cristagalli agglutinin

5. Affinity of four immobilized Erythrina lectins toward various n-linked glycopeptides and related oligosaccharides

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