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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...

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Autores principales: Liu, Yu-Ching, Chen, Chao-Jung, Lee, Miau-Rong, Li, Mi, Hsieh, Wen-Tsong, Chung, Jing-Gung, Ho, Heng-Chien
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
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.
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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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