Analysis of proteins by agarose native gel electrophoresis in the presence of solvent additives

Solvent additives, including NaCl, arginine hydrochloride (ArgHCl), glycine and sucrose, are used to enhance protein stability or reduce protein aggregation. Here, we studied the effects of these additives on proteins using agarose native gel electrophoresis. Since these additives are used at relati...

Full description

Saved in:
Bibliographic Details
Published in:International journal of biological macromolecules 2022-02, Vol.198, p.26-36
Main Authors: Tomioka, Yui, Arakawa, Tsutomu, Akuta, Teruo, Nakagawa, Masataka, Ishibashi, Matsujiro
Format: Article
Language:English
Subjects:
Agarose native gel
Arginine
Muramidase
Soluble aggregates
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c434t-b2797b579d63bf4a29eab9cb54e08f55f9a9858b7a4702e81e57926fe906e8d23
cites cdi_FETCH-LOGICAL-c434t-b2797b579d63bf4a29eab9cb54e08f55f9a9858b7a4702e81e57926fe906e8d23
container_end_page 36
container_issue
container_start_page 26
container_title International journal of biological macromolecules
container_volume 198
creator Tomioka, Yui
Arakawa, Tsutomu
Akuta, Teruo
Nakagawa, Masataka
Ishibashi, Matsujiro
description Solvent additives, including NaCl, arginine hydrochloride (ArgHCl), glycine and sucrose, are used to enhance protein stability or reduce protein aggregation. Here, we studied the effects of these additives on proteins using agarose native gel electrophoresis. Since these additives are used at relatively high concentration, we first confirmed that they do not interfere with the performance of the native gel electrophoresis. Agarose native gel electrophoresis showed that aggregation of bovine serum albumin (BSA) induced by heating was slightly reduced by NaCl and ArgHCl. On the contrary, glycine and sucrose had marginal effects. ArgHCl and NaCl promoted heat aggregation of monoclonal antibody (mAb), while glycine and sucrose stabilized the native mAb. Arginine methyl ester inhibited heat aggregation of lysozyme and, to a much lesser extent, BSA. These results show that agarose native gel electrophoresis can be used to analyze the effects of solvent additives on proteins subjected to heat stresses. SYPRO Orange that stains only unfolded proteins confirmed unfolded structures of soluble aggregates.
doi_str_mv 10.1016/j.ijbiomac.2021.12.084
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2614761713</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0141813021027148</els_id><sourcerecordid>2614761713</sourcerecordid><originalsourceid>FETCH-LOGICAL-c434t-b2797b579d63bf4a29eab9cb54e08f55f9a9858b7a4702e81e57926fe906e8d23</originalsourceid><addsrcrecordid>eNqFkMtqwzAQRUVpadK0vxC07MauJMu2tGsIfUGgm3YtJHucyDhWKjmB_H1lknTb1cBwzwz3IDSnJKWEFk9taltj3VZXKSOMppSlRPArNKWilAkhJLtGU0I5TQTNyATdhdDGbZFTcYsmGZc5Z1JMkVr0ujsGG7Br8M67AWwfsDlivdbeBcC9HuwB8Bo6DB1Ug3e7jfMwErbHwwYiBQH6CsYLwXUH6Aes69qOXLhHN43uAjyc5wx9v758Ld-T1efbx3KxSiqe8SExrJSlyUtZF5lpuGYStJGVyTkQ0eR5I7UUuTCl5iVhICjELCsakKQAUbNshh5Pd2OHnz2EQW1tqKDrdA9uHxQrKC8LWtIsRotTtIoFg4dG7bzdan9UlKhRrmrVRa4a5SrKVJQbwfn5x95sof7DLjZj4PkUgNj0YMGrUNlRTW19VKdqZ__78QsFVI-Z</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2614761713</pqid></control><display><type>article</type><title>Analysis of proteins by agarose native gel electrophoresis in the presence of solvent additives</title><source>ScienceDirect Freedom Collection</source><creator>Tomioka, Yui ; Arakawa, Tsutomu ; Akuta, Teruo ; Nakagawa, Masataka ; Ishibashi, Matsujiro</creator><creatorcontrib>Tomioka, Yui ; Arakawa, Tsutomu ; Akuta, Teruo ; Nakagawa, Masataka ; Ishibashi, Matsujiro</creatorcontrib><description>Solvent additives, including NaCl, arginine hydrochloride (ArgHCl), glycine and sucrose, are used to enhance protein stability or reduce protein aggregation. Here, we studied the effects of these additives on proteins using agarose native gel electrophoresis. Since these additives are used at relatively high concentration, we first confirmed that they do not interfere with the performance of the native gel electrophoresis. Agarose native gel electrophoresis showed that aggregation of bovine serum albumin (BSA) induced by heating was slightly reduced by NaCl and ArgHCl. On the contrary, glycine and sucrose had marginal effects. ArgHCl and NaCl promoted heat aggregation of monoclonal antibody (mAb), while glycine and sucrose stabilized the native mAb. Arginine methyl ester inhibited heat aggregation of lysozyme and, to a much lesser extent, BSA. These results show that agarose native gel electrophoresis can be used to analyze the effects of solvent additives on proteins subjected to heat stresses. SYPRO Orange that stains only unfolded proteins confirmed unfolded structures of soluble aggregates.</description><identifier>ISSN: 0141-8130</identifier><identifier>ISSN: 1879-0003</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2021.12.084</identifier><identifier>PMID: 34954298</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Agarose native gel ; Arginine ; Muramidase ; Soluble aggregates</subject><ispartof>International journal of biological macromolecules, 2022-02, Vol.198, p.26-36</ispartof><rights>2021 Elsevier B.V.</rights><rights>Copyright © 2021 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-b2797b579d63bf4a29eab9cb54e08f55f9a9858b7a4702e81e57926fe906e8d23</citedby><cites>FETCH-LOGICAL-c434t-b2797b579d63bf4a29eab9cb54e08f55f9a9858b7a4702e81e57926fe906e8d23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34954298$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tomioka, Yui</creatorcontrib><creatorcontrib>Arakawa, Tsutomu</creatorcontrib><creatorcontrib>Akuta, Teruo</creatorcontrib><creatorcontrib>Nakagawa, Masataka</creatorcontrib><creatorcontrib>Ishibashi, Matsujiro</creatorcontrib><title>Analysis of proteins by agarose native gel electrophoresis in the presence of solvent additives</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>Solvent additives, including NaCl, arginine hydrochloride (ArgHCl), glycine and sucrose, are used to enhance protein stability or reduce protein aggregation. Here, we studied the effects of these additives on proteins using agarose native gel electrophoresis. Since these additives are used at relatively high concentration, we first confirmed that they do not interfere with the performance of the native gel electrophoresis. Agarose native gel electrophoresis showed that aggregation of bovine serum albumin (BSA) induced by heating was slightly reduced by NaCl and ArgHCl. On the contrary, glycine and sucrose had marginal effects. ArgHCl and NaCl promoted heat aggregation of monoclonal antibody (mAb), while glycine and sucrose stabilized the native mAb. Arginine methyl ester inhibited heat aggregation of lysozyme and, to a much lesser extent, BSA. These results show that agarose native gel electrophoresis can be used to analyze the effects of solvent additives on proteins subjected to heat stresses. SYPRO Orange that stains only unfolded proteins confirmed unfolded structures of soluble aggregates.</description><subject>Agarose native gel</subject><subject>Arginine</subject><subject>Muramidase</subject><subject>Soluble aggregates</subject><issn>0141-8130</issn><issn>1879-0003</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNqFkMtqwzAQRUVpadK0vxC07MauJMu2tGsIfUGgm3YtJHucyDhWKjmB_H1lknTb1cBwzwz3IDSnJKWEFk9taltj3VZXKSOMppSlRPArNKWilAkhJLtGU0I5TQTNyATdhdDGbZFTcYsmGZc5Z1JMkVr0ujsGG7Br8M67AWwfsDlivdbeBcC9HuwB8Bo6DB1Ug3e7jfMwErbHwwYiBQH6CsYLwXUH6Aes69qOXLhHN43uAjyc5wx9v758Ld-T1efbx3KxSiqe8SExrJSlyUtZF5lpuGYStJGVyTkQ0eR5I7UUuTCl5iVhICjELCsakKQAUbNshh5Pd2OHnz2EQW1tqKDrdA9uHxQrKC8LWtIsRotTtIoFg4dG7bzdan9UlKhRrmrVRa4a5SrKVJQbwfn5x95sof7DLjZj4PkUgNj0YMGrUNlRTW19VKdqZ__78QsFVI-Z</recordid><startdate>20220215</startdate><enddate>20220215</enddate><creator>Tomioka, Yui</creator><creator>Arakawa, Tsutomu</creator><creator>Akuta, Teruo</creator><creator>Nakagawa, Masataka</creator><creator>Ishibashi, Matsujiro</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20220215</creationdate><title>Analysis of proteins by agarose native gel electrophoresis in the presence of solvent additives</title><author>Tomioka, Yui ; Arakawa, Tsutomu ; Akuta, Teruo ; Nakagawa, Masataka ; Ishibashi, Matsujiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-b2797b579d63bf4a29eab9cb54e08f55f9a9858b7a4702e81e57926fe906e8d23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Agarose native gel</topic><topic>Arginine</topic><topic>Muramidase</topic><topic>Soluble aggregates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tomioka, Yui</creatorcontrib><creatorcontrib>Arakawa, Tsutomu</creatorcontrib><creatorcontrib>Akuta, Teruo</creatorcontrib><creatorcontrib>Nakagawa, Masataka</creatorcontrib><creatorcontrib>Ishibashi, Matsujiro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tomioka, Yui</au><au>Arakawa, Tsutomu</au><au>Akuta, Teruo</au><au>Nakagawa, Masataka</au><au>Ishibashi, Matsujiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of proteins by agarose native gel electrophoresis in the presence of solvent additives</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2022-02-15</date><risdate>2022</risdate><volume>198</volume><spage>26</spage><epage>36</epage><pages>26-36</pages><issn>0141-8130</issn><issn>1879-0003</issn><eissn>1879-0003</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Solvent additives, including NaCl, arginine hydrochloride (ArgHCl), glycine and sucrose, are used to enhance protein stability or reduce protein aggregation. Here, we studied the effects of these additives on proteins using agarose native gel electrophoresis. Since these additives are used at relatively high concentration, we first confirmed that they do not interfere with the performance of the native gel electrophoresis. Agarose native gel electrophoresis showed that aggregation of bovine serum albumin (BSA) induced by heating was slightly reduced by NaCl and ArgHCl. On the contrary, glycine and sucrose had marginal effects. ArgHCl and NaCl promoted heat aggregation of monoclonal antibody (mAb), while glycine and sucrose stabilized the native mAb. Arginine methyl ester inhibited heat aggregation of lysozyme and, to a much lesser extent, BSA. These results show that agarose native gel electrophoresis can be used to analyze the effects of solvent additives on proteins subjected to heat stresses. SYPRO Orange that stains only unfolded proteins confirmed unfolded structures of soluble aggregates.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>34954298</pmid><doi>10.1016/j.ijbiomac.2021.12.084</doi><tpages>11</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0141-8130
ispartof International journal of biological macromolecules, 2022-02, Vol.198, p.26-36
issn 0141-8130
1879-0003
1879-0003
language eng
recordid cdi_proquest_miscellaneous_2614761713
source ScienceDirect Freedom Collection
subjects Agarose native gel
Arginine
Muramidase
Soluble aggregates
title Analysis of proteins by agarose native gel electrophoresis in the presence of solvent additives
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-21T19%3A38%3A24IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Analysis%20of%20proteins%20by%20agarose%20native%20gel%20electrophoresis%20in%20the%20presence%20of%20solvent%20additives&rft.jtitle=International%20journal%20of%20biological%20macromolecules&rft.au=Tomioka,%20Yui&rft.date=2022-02-15&rft.volume=198&rft.spage=26&rft.epage=36&rft.pages=26-36&rft.issn=0141-8130&rft.eissn=1879-0003&rft_id=info:doi/10.1016/j.ijbiomac.2021.12.084&rft_dat=%3Cproquest_cross%3E2614761713%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c434t-b2797b579d63bf4a29eab9cb54e08f55f9a9858b7a4702e81e57926fe906e8d23%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2614761713&rft_id=info:pmid/34954298&rfr_iscdi=true