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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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 |
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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. |
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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 |
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2014 |
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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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