Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families

This paper describes an efficient method of studying the glycoproteins found in snake venom. The glycosylation profiles of the Elapidae and Viperidae snake families were analyzed using FITC-labeled lectin glycoconjugates. The Con A-agarose affinity enrichment technique was used to fractionate glycop...

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Main Authors: Nawarak J., Phutrakul S., Chen S.-T.
Format: Article
Language:English
Published: 2014
Online Access:http://www.scopus.com/inward/record.url?eid=2-s2.0-4444279812&partnerID=40&md5=e417d44c2e31beef14e935ddccb5b6d5
http://cmuir.cmu.ac.th/handle/6653943832/7191
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Institution: Chiang Mai University
Language: English
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spelling th-cmuir.6653943832-71912014-08-30T03:51:40Z Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families Nawarak J. Phutrakul S. Chen S.-T. This paper describes an efficient method of studying the glycoproteins found in snake venom. The glycosylation profiles of the Elapidae and Viperidae snake families were analyzed using FITC-labeled lectin glycoconjugates. The Con A-agarose affinity enrichment technique was used to fractionate glycoproteins from the N. naja kaouthia venom. The results revealed a large number of Con A binding glycoproteins, most of which have moderate to high molecular weights. To identify the proteins, the isolated glycoprotein fractions were subjected to two-dimensional electrophoresis and MALDI-TOF MS. Protein sequences were compared with published protein databases to determine for their biological functions. 2014-08-30T03:51:40Z 2014-08-30T03:51:40Z 2004 Article 15353893 10.1021/pr034052+ 15253418 JPROB http://www.scopus.com/inward/record.url?eid=2-s2.0-4444279812&partnerID=40&md5=e417d44c2e31beef14e935ddccb5b6d5 http://cmuir.cmu.ac.th/handle/6653943832/7191 English
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
language English
description This paper describes an efficient method of studying the glycoproteins found in snake venom. The glycosylation profiles of the Elapidae and Viperidae snake families were analyzed using FITC-labeled lectin glycoconjugates. The Con A-agarose affinity enrichment technique was used to fractionate glycoproteins from the N. naja kaouthia venom. The results revealed a large number of Con A binding glycoproteins, most of which have moderate to high molecular weights. To identify the proteins, the isolated glycoprotein fractions were subjected to two-dimensional electrophoresis and MALDI-TOF MS. Protein sequences were compared with published protein databases to determine for their biological functions.
format Article
author Nawarak J.
Phutrakul S.
Chen S.-T.
spellingShingle Nawarak J.
Phutrakul S.
Chen S.-T.
Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families
author_facet Nawarak J.
Phutrakul S.
Chen S.-T.
author_sort Nawarak J.
title Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families
title_short Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families
title_full Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families
title_fullStr Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families
title_full_unstemmed Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families
title_sort analysis of lectin-bound glycoproteins in snake venom from the elapidae and viperidae families
publishDate 2014
url http://www.scopus.com/inward/record.url?eid=2-s2.0-4444279812&partnerID=40&md5=e417d44c2e31beef14e935ddccb5b6d5
http://cmuir.cmu.ac.th/handle/6653943832/7191
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