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Purification and Characterization of a Novel β-d-Galactosides-Specific Lectin from Clitoria ternatea
- Source :
- The Protein Journal. 26:403-413
- Publication Year :
- 2007
- Publisher :
- Springer Science and Business Media LLC, 2007.
-
Abstract
- A lectin present in seeds of Clitoria ternatea agglutinated trypsin-treated human B erythrocytes. The sugar specificity assay indicated that lectin belongs to Gal/Gal NAc-specific group. Hence the lectin, designated C. ternatea agglutinin (CTA), was purified by the combination of acetic acid precipitation, salt fractionation and affinity chromatography. HPLC gel filtration, SDS-polyacrylamide gel electrophoresis and mass spectrometry indicated that the native lectin is composed of two identical subunits of molecular weight 34.7 kDa associated by non covalent bonds. The N-terminal sequence of CTA shared homology with Glycine max and Pisum sativum. Complete sequence was also found to be homologous to S-64 protein of Glycine max, suggesting that CTA probably exhibits both hemagglutination and probably sugar uptake activity. The carbohydrate binding specificity of the lectin was investigated by quantitative turbidity measurements, and percent inhibition assays. Based on these assays, we conclude that CTA binds beta-D: -galactosides, and also may has an extended specificity towards non-reducing terminal Neu5Acalpha2,6Gal.
- Subjects :
- Spectrometry, Mass, Electrospray Ionization
Molecular Sequence Data
Molecular Conformation
Enzyme-Linked Immunosorbent Assay
Bioengineering
Biochemistry
Chromatography, Affinity
Analytical Chemistry
Agglutinin
Affinity chromatography
Galactosides
Lectins
Humans
Amino Acid Sequence
Peptide sequence
Polyacrylamide gel electrophoresis
Chromatography, High Pressure Liquid
Gel electrophoresis
biology
Circular Dichroism
Clitoria ternatea
Organic Chemistry
Lectin
Hemagglutination Tests
biology.organism_classification
Chromatography, Gel
biology.protein
Electrophoresis, Polyacrylamide Gel
Clitoria
Subjects
Details
- ISSN :
- 18758355 and 15723887
- Volume :
- 26
- Database :
- OpenAIRE
- Journal :
- The Protein Journal
- Accession number :
- edsair.doi.dedup.....084a6083f8031af6dfa51471abc6e52c