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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
An alternate high yielding purification method for Clitoria ternatea lectin
Aabgeena Naeem1, Ejaz Ahmad, Rizwan Hasan Khan
1Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India; Department of Biochemistry, Life Science, AMU, Aligarh 202002, India.
International Journal of Biological Macromolecules
|June 26, 2007
Summary
A new method using asialofetuin agarose columns significantly improves the yield of Clitoria ternatea agglutinin (CTA). This lectin is valuable for glycobiology, biomedical, and cancer research.
Area of Science:
- Biochemistry
- Molecular Biology
- Biomedical Research
Background:
- Clitoria ternatea agglutinin (CTA) purified previously binds beta-d-galactosides.
- CTA is a valuable tool for glycobiology, biomedical, and cancer research.
Purpose of the Study:
- To develop a high-yielding purification method for Clitoria ternatea agglutinin (CTA).
- To compare the efficacy of asialofetuin CL agarose with fetuin CL agarose for CTA purification.
Main Methods:
- Affinity chromatography using asialofetuin CL agarose column.
- Analysis of purified lectin using SDS-PAGE, HPLC, and N-terminal sequencing.
Main Results:
- A new lectin, CTL, was purified using asialofetuin CL agarose.
- The lectin content was 30mg/30g dry weight.
- The yield of CTL (2.8%) was significantly higher than CTA (0.3%).
- Purified CTL showed similarity to CTA in SDS pattern, HPLC, and N-terminal sequence.
Conclusions:
- Asialofetuin CL agarose is a more efficient method for purifying Clitoria ternatea agglutinin.
- The enhanced yield facilitates broader applications of CTA in research.
