Strong affinity ofMaackia amurensishemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A-Reference-Cited by-同舟云学术

Strong affinity ofMaackia amurensishemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A

Published:1994-04-11 Issue:3 Volume:342 Page:334-338
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Konami Yukiko,Yamamoto Kazuo,Osawa Toshiaki,Irimura Taturo

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)80527-X/fullpdf

Reference27 articles.

1. Studies on Hemagglutinins from Maackia amurensis Seeds

2. Competitive binding of lectins to human erythrocytes

3. Elucidation of lectin receptors by quantitative inhibition of lectin binding to human erythrocytes and lymphocytes

4. The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2,3 to penultimate galactose residues.

5. Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins.

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