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Journal of Biological Sciences
  Year: 2009 | Volume: 9 | Issue: 4 | Page No.: 319-325
DOI: 10.3923/jbs.2009.319.325
 
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Purification and Characterization of a D-Galactoside-Binding Lectin Purified from Bladder Moon Shell (Glossaulax didyma Roding)

Y. Fujii, S.M.A. Kawsar, R. Matsumoto, H. Yasumitsu, N. Kojima and Y. Ozeki

Abstract:
To find novel carbohydrate-binding proteins (lectins) from marine invertebrates to understand the binding mechanism of the protein and to apply it for glycan-dependent diagnostics and/or glycoconjugates capture technology. A D-galactoside-binding lectin was purified from foot of bladder moon shell, Glossaulax didyma by lactosyl-agarose affinity chromatography. The crude supernatant by Tris-buffered saline had strong hemagglutination activity against trypsinized and glutaraldehyde-fixed human erythrocyte. However, the activity was not inhibited by any tested saccharides and chilete reagents. On the other hand, the dialyzed crude supernatant obtained from the precipitates with 100 mM lactose in Tris-buffered saline had also hemagglutination activity inhibited by β-galactoside and D-galactose. The lectin was purified with lactosyl-agarose affinity chromatography. The molecular mass of the lectin was determined to be 60 kDa by SDS-PAGE under reducing and non-reducing conditions and being a 60 kDa polypeptide monomer by gel permeation chromatography. The association-rate constant (kass) and dissociation-rate constant (kdiss) determined for the lectin against asialofetuin was determined as 5.4x104 M-1sec-1 and 7.2x10-3sec-1, respectively. Lectin-conjugated Sepharose gel captured asialofetuin and eluted it by lactose-containing buffer from the gel, indicating that the lectin could catch the asialoglycoprotein. It was concluded that a many amount of a D-galactoside-binding lectin which can catch asialoglycoprotein presents in foot of the bladder moon shell.
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How to cite this article:

Y. Fujii, S.M.A. Kawsar, R. Matsumoto, H. Yasumitsu, N. Kojima and Y. Ozeki, 2009. Purification and Characterization of a D-Galactoside-Binding Lectin Purified from Bladder Moon Shell (Glossaulax didyma Roding). Journal of Biological Sciences, 9: 319-325.

DOI: 10.3923/jbs.2009.319.325

URL: https://scialert.net/abstract/?doi=jbs.2009.319.325

COMMENTS
15 March, 2009
Dr. A. K. M. Lutfur:

This article is new method to purify novel lectins from marine invertebrates. Thanks to authors.
19 March, 2009
Yasuhiro Ozeki:
Thank you for your attention to our article. Lectins in marine invertebrates should be interested by audiences in the journal, because it expects to be able to discover new molecule with various different carbohydrate binding properties. Our method using carbohydrate-conjugated affinity chromatography is a representative procedure for lectin purification. However, the point, as we used it for the purification of lectin in marine invertebrates and succeeded to isolate a new lectin with attractive biochemical properties is emphasised in the article. Best.
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