Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection

Most of commercial latex products originated from natural rubber produced by Hevea brasiliensis. Hevea latex contained of rubber particles that are linked with numerous allergens protein. The allergens protein associates with rubber particles can cause allergic reaction that range from contact and...

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Main Authors: Nurul Faziha I.,, Shamsul Bahri A.R.,, Suhaizan L.,, Iffah Hazirah M.N.,, Ngadin A.A.,
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 2017
Online Access:http://journalarticle.ukm.my/12381/1/46_03_29.pdf
http://journalarticle.ukm.my/12381/
http://mabjournal.com/index.php?option=com_content&view=article&id=674&catid=59:current-view&Itemid=56
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spelling my-ukm.journal.123812018-11-30T22:46:02Z http://journalarticle.ukm.my/12381/ Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection Nurul Faziha I., Shamsul Bahri A.R., Suhaizan L., Iffah Hazirah M.N., Ngadin A.A., Most of commercial latex products originated from natural rubber produced by Hevea brasiliensis. Hevea latex contained of rubber particles that are linked with numerous allergens protein. The allergens protein associates with rubber particles can cause allergic reaction that range from contact and systemic urticarial to asthma, anaplyaxis and even death. Although allergen proteins are well known to be involved in rubber synthesis of H. brasiliensis, their presence in this species as well as other Hevea species is still need to be determined. For sustainability production of high demanding commercial latex, this study is conducted to investigate the protein profiling of two allergens on eight Hevea species obtained from the 1995 germplasm collection. Latex collected from eight Hevea species were prepared to detect allergens protein of Hevb1 and Hevb3 using SDS Polyacrylamide Gel (SDS-PAGE). Immunoblotting technique was used to evaluate compatibility of allergens protein to bind with monoclonal and polyclonal antisera. The results showed that both of Hevb1 and Hevb3 proteins were detected in eight Hevea species. However, Hevb1 and Hevb3 proteins showed different ability in binding the monoclonal and polyclonal antisera. Data on protein profiling of eight Hevea species constitute a potential source of good trait in future plant breeding or as a key to have a future rubber tree with less or allergen free latex. Penerbit Universiti Kebangsaan Malaysia 2017-10 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/12381/1/46_03_29.pdf Nurul Faziha I., and Shamsul Bahri A.R., and Suhaizan L., and Iffah Hazirah M.N., and Ngadin A.A., (2017) Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection. Malaysian Applied Biology, 46 (3). pp. 239-245. ISSN 0126-8643 http://mabjournal.com/index.php?option=com_content&view=article&id=674&catid=59:current-view&Itemid=56
institution Universiti Kebangsaan Malaysia
building Perpustakaan Tun Sri Lanang Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Kebangsaan Malaysia
content_source UKM Journal Article Repository
url_provider http://journalarticle.ukm.my/
language English
description Most of commercial latex products originated from natural rubber produced by Hevea brasiliensis. Hevea latex contained of rubber particles that are linked with numerous allergens protein. The allergens protein associates with rubber particles can cause allergic reaction that range from contact and systemic urticarial to asthma, anaplyaxis and even death. Although allergen proteins are well known to be involved in rubber synthesis of H. brasiliensis, their presence in this species as well as other Hevea species is still need to be determined. For sustainability production of high demanding commercial latex, this study is conducted to investigate the protein profiling of two allergens on eight Hevea species obtained from the 1995 germplasm collection. Latex collected from eight Hevea species were prepared to detect allergens protein of Hevb1 and Hevb3 using SDS Polyacrylamide Gel (SDS-PAGE). Immunoblotting technique was used to evaluate compatibility of allergens protein to bind with monoclonal and polyclonal antisera. The results showed that both of Hevb1 and Hevb3 proteins were detected in eight Hevea species. However, Hevb1 and Hevb3 proteins showed different ability in binding the monoclonal and polyclonal antisera. Data on protein profiling of eight Hevea species constitute a potential source of good trait in future plant breeding or as a key to have a future rubber tree with less or allergen free latex.
format Article
author Nurul Faziha I.,
Shamsul Bahri A.R.,
Suhaizan L.,
Iffah Hazirah M.N.,
Ngadin A.A.,
spellingShingle Nurul Faziha I.,
Shamsul Bahri A.R.,
Suhaizan L.,
Iffah Hazirah M.N.,
Ngadin A.A.,
Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection
author_facet Nurul Faziha I.,
Shamsul Bahri A.R.,
Suhaizan L.,
Iffah Hazirah M.N.,
Ngadin A.A.,
author_sort Nurul Faziha I.,
title Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection
title_short Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection
title_full Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection
title_fullStr Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection
title_full_unstemmed Protein profiling of Hevb1 and Hevb3 in Hevea species obtained from the 1995 germplasm collection
title_sort protein profiling of hevb1 and hevb3 in hevea species obtained from the 1995 germplasm collection
publisher Penerbit Universiti Kebangsaan Malaysia
publishDate 2017
url http://journalarticle.ukm.my/12381/1/46_03_29.pdf
http://journalarticle.ukm.my/12381/
http://mabjournal.com/index.php?option=com_content&view=article&id=674&catid=59:current-view&Itemid=56
_version_ 1643738772673658880
score 13.211869