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Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates
Numerous reports illustrate the diverse effects of chewing the areca nut, most of which are harmful and have been shown to be associated with oral cancer. Nearly all of the studies are focused on the extract and/or low molecular weight ingredients in the areca nut. The purpose of this report is to i...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821912/ https://www.ncbi.nlm.nih.gov/pubmed/24250715 http://dx.doi.org/10.1155/2013/412851 |
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author | Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien |
author_facet | Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien |
author_sort | Liu, Yu-Ching |
collection | PubMed |
description | Numerous reports illustrate the diverse effects of chewing the areca nut, most of which are harmful and have been shown to be associated with oral cancer. Nearly all of the studies are focused on the extract and/or low molecular weight ingredients in the areca nut. The purpose of this report is to identify the major protein component in the areca nut. After ammonium sulfate fractionation, the concentrated areca nut extract is subjected to DEAE-cellulose chromatography. A colored protein is eluted at low NaCl concentration and the apparently homogeneous eluent represents the major protein component compared to the areca nut extract. The colored protein shares partial sequence identity with the royal palm tree peroxidase and its peroxidase activity is confirmed using an established assay. In the study, the natural substrates of areca nut peroxidase are identified as catechin, epicatechin, and procyanidin B1. The two former substrates are similarly oxidized to form a 576 Da product with concomitant removal of four hydrogen atoms. Interestingly, oxidation of procyanidin B1 occurs only in the presence of catechin or epicatechin and an additional product with an 864 Da molecular mass. In addition, procyanidin B1 is identified as a peroxidase substrate for the first time. |
format | Online Article Text |
id | pubmed-3821912 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-38219122013-11-18 Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien Evid Based Complement Alternat Med Research Article Numerous reports illustrate the diverse effects of chewing the areca nut, most of which are harmful and have been shown to be associated with oral cancer. Nearly all of the studies are focused on the extract and/or low molecular weight ingredients in the areca nut. The purpose of this report is to identify the major protein component in the areca nut. After ammonium sulfate fractionation, the concentrated areca nut extract is subjected to DEAE-cellulose chromatography. A colored protein is eluted at low NaCl concentration and the apparently homogeneous eluent represents the major protein component compared to the areca nut extract. The colored protein shares partial sequence identity with the royal palm tree peroxidase and its peroxidase activity is confirmed using an established assay. In the study, the natural substrates of areca nut peroxidase are identified as catechin, epicatechin, and procyanidin B1. The two former substrates are similarly oxidized to form a 576 Da product with concomitant removal of four hydrogen atoms. Interestingly, oxidation of procyanidin B1 occurs only in the presence of catechin or epicatechin and an additional product with an 864 Da molecular mass. In addition, procyanidin B1 is identified as a peroxidase substrate for the first time. Hindawi Publishing Corporation 2013 2013-10-24 /pmc/articles/PMC3821912/ /pubmed/24250715 http://dx.doi.org/10.1155/2013/412851 Text en Copyright © 2013 Yu-Ching Liu et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates |
title | Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates |
title_full | Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates |
title_fullStr | Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates |
title_full_unstemmed | Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates |
title_short | Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates |
title_sort | peroxidase as the major protein constituent in areca nut and identification of its natural substrates |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821912/ https://www.ncbi.nlm.nih.gov/pubmed/24250715 http://dx.doi.org/10.1155/2013/412851 |
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