Abstract:
:In our previous publication we had reported the purification and characterization of Clitoria ternatea agglutinin from its seeds on fetuin CL agarose affinity column, designated CTA [A. Naeem, S. Haque, R.H. Khan. Protein J., 2007]. Since CTA binds beta-d-galactosides, this lectin can be used as valuable tool for glycobiology studies in biomedical and cancer research. So an attempt was made for a high yielding alternative purification method employing the use of asialofetuin CL agarose column for the above-mentioned lectin, designated CTL. The fetuin affinity purified agglutinin was found similar to asialofetuin affinity purified lectin in SDS pattern, HPLC and N-terminal sequence. The content of lectin was found to be 30mg/30g dry weight of pulse. The yield was 2.8% as compared to 0.3% obtained on fetuin column. The number of tryptophan and tyrosine estimated was four and six per subunit.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Naeem A,Ahmad E,Khan RHdoi
10.1016/j.ijbiomac.2007.05.006subject
Has Abstractpub_date
2007-10-01 00:00:00pages
481-6issue
4eissn
0141-8130issn
1879-0003pii
S0141-8130(07)00133-Xjournal_volume
41pub_type
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