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Purification of an antigenic glycopeptide from buffalo colostrum.

Aparna, H. S. and Salimath, P. V. (2001) Purification of an antigenic glycopeptide from buffalo colostrum. Journal of Food Science and Technology, 38 (5). 450-452, 27 ref..

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Purification and characterization of a glycopeptide from buffalo colostrum is described. The sialoglycopeptide was fractionated and purified on Sephadex G-25 and QAE-Sephadex A-25. Its homogeneity was confirmed by RP-HPLC and electrophoresis. It consisted of NeuNAc, Fuc, Gal, Man, GlcNAc in the ratio 1:1:2:1:1 and Asp, Glu, Ser, Thr, Pro as major amino acids. Lys was found to be the N-terminal amino acid residue. Antibodies raised to the glycopeptide were immunogenic and were similar to blood group-A substance as determined by immunodouble diffusion and haemagglutination techniques.

Item Type: Article
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 25 Peptide Chemistry
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 01 Jun 2011 07:17
Last Modified: 28 Dec 2011 09:59
URI: http://ir.cftri.com/id/eprint/7624

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