Soluble 14-kDa beta-galactoside-specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain.-Reference-Cited by-同舟云学术

Soluble 14-kDa beta-galactoside-specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain.

Published:1991-03 Issue:9 Volume:266 Page:5552-5557
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Abbott W M,Feizi T

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference32 articles.

1. Evidence that the 14 kDa soluble β-galactoside-binding lectin in man is encoded by a single gene

2. Further studies of oligosaccharide recognition by the soluble 13 kDa lectin of bovine heart muscle. Ability to accommodate the blood-group-H and -B-related sequences

3. Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein

4. An IgE-binding protein with a distinctive repetitive sequence and homology with an IgG receptor.

5. Vertebrate lectins, Comparison of properties of beta-galactoside-binding lectins from tissues of calf and chicken.

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