Further characterisation of sialic acid-binding lectin from the horseshoe crab Carcino scorpias rotunda cauda.

Thambi Dorai, D. and Bachhawat, B. K. and Bishayee, S. and Kannan, K. and Rajagopal Rao, D. (1981) Further characterisation of sialic acid-binding lectin from the horseshoe crab Carcino scorpias rotunda cauda. Archives of Biochemistry and Biophysics, 209. pp. 325-333.

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Abstract

A sialic acid-binding lectin, named carcinoscorpin, has been isolated from the horseshoe crab Carcinoscorpius rotunda caudu It is a glycoprotein of molecular-weight 420,000, having two subunits of molecular weight 2’7,000 and 28,000, both subunits responding to glycoprotein stain. Leucine was detected as the only NH,-terminal amino acid. The sedimentation constant of the native lectin was found to be 12.7 s. On digestion with trypsin, the lectin gave 18 soluble tryptic peptides. This lectin was found to be antigenically unrelated to another sialic acid-binding lectin, limulin, isolated from the horseshoe crab Limulus polyphemus. A lectin-specific disaccharide alcohol namely 0-(N-acetylneuraminyl) (2 + 6)2- acetamido-2-deoxy-~galactitol was found to quench the typical tryptophan fluorescence of the native lectin at 332 nm. The association constant for this interaction was determined spectrofluorimetrically and found to be 1.82 x 103 M-l.

Item Type:	Article
Uncontrolled Keywords:	carcinoscorpin, lectins
Subjects:	600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins 600 Technology > 08 Food technology > 28 Meat, Fish & Poultry
Divisions:	Dept. of Biochemistry
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	09 Mar 2011 07:28
Last Modified:	30 Apr 2012 05:45
URI:	http://ir.cftri.res.in/id/eprint/4272

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