Urea can inhibit efficient reduction and alkylation of protein dimers in solution demonstrated by the beta subunit of alpha glucosidase II.
Identifieur interne : 001F88 ( Ncbi/Merge ); précédent : 001F87; suivant : 001F89Urea can inhibit efficient reduction and alkylation of protein dimers in solution demonstrated by the beta subunit of alpha glucosidase II.
Auteurs : Meena Kumari [États-Unis] ; Antje Anji [États-Unis]Source :
- Analytical biochemistry [ 1096-0309 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Urea, alpha-Glucosidases.
- chemical , metabolism : alpha-Glucosidases.
- methods : Electrophoresis, Gel, Two-Dimensional, Mass Spectrometry.
- Alkylation, Animals, Brain Chemistry, Mice, Protein Multimerization.
Abstract
Protein reduction and alkylation is routinely used for analysis of protein dimers and protein complexes in cell fractions using two dimensional gel electrophoresis and mass spectrometry. To resolve the heterogeneity of a high molecular weight protein band that is highlighted by an antibody to the beta subunit of alpha glucosidase II (GIIβ), we performed reduction and alkylation of cytosolic proteins extracted from mouse brain. The presence of urea in the reduction/alkylation buffer inhibited the chemical processes. It is thus recommended that protein reduction/alkylation be performed both in the presence and absence of urea for the separation of mono-/hetero-mers.
DOI: 10.1016/j.ab.2018.10.008
PubMed: 30312619
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To resolve the heterogeneity of a high molecular weight protein band that is highlighted by an antibody to the beta subunit of alpha glucosidase II (GIIβ), we performed reduction and alkylation of cytosolic proteins extracted from mouse brain. The presence of urea in the reduction/alkylation buffer inhibited the chemical processes. It is thus recommended that protein reduction/alkylation be performed both in the presence and absence of urea for the separation of mono-/hetero-mers.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30312619</PMID><DateCompleted><Year>2019</Year><Month>11</Month><Day>27</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>27</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0309</ISSN><JournalIssue CitedMedium="Internet"><Volume>566</Volume><PubDate><Year>2019</Year><Month>02</Month><Day>01</Day></PubDate></JournalIssue><Title>Analytical biochemistry</Title><ISOAbbreviation>Anal. Biochem.</ISOAbbreviation></Journal><ArticleTitle>Urea can inhibit efficient reduction and alkylation of protein dimers in solution demonstrated by the beta subunit of alpha glucosidase II.</ArticleTitle><Pagination><MedlinePgn>20-22</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0003-2697(18)30673-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ab.2018.10.008</ELocationID><Abstract><AbstractText>Protein reduction and alkylation is routinely used for analysis of protein dimers and protein complexes in cell fractions using two dimensional gel electrophoresis and mass spectrometry. To resolve the heterogeneity of a high molecular weight protein band that is highlighted by an antibody to the beta subunit of alpha glucosidase II (GIIβ), we performed reduction and alkylation of cytosolic proteins extracted from mouse brain. The presence of urea in the reduction/alkylation buffer inhibited the chemical processes. It is thus recommended that protein reduction/alkylation be performed both in the presence and absence of urea for the separation of mono-/hetero-mers.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kumari</LastName><ForeName>Meena</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Anatomy and Physiology, College of Veterinary Medicine, Kansas State University, 231Coles Hall, Manhattan, KS, 66506, USA. Electronic address: mkumari@vet.ksu.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Anji</LastName><ForeName>Antje</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Anatomy and Physiology, College of Veterinary Medicine, Kansas State University, 231Coles Hall, Manhattan, KS, 66506, USA. Electronic address: aanji@vet.ksu.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>10</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Anal Biochem</MedlineTA><NlmUniqueID>0370535</NlmUniqueID><ISSNLinking>0003-2697</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>8W8T17847W</RegistryNumber><NameOfSubstance UI="D014508">Urea</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.20</RegistryNumber><NameOfSubstance UI="D000520">alpha-Glucosidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000478" MajorTopicYN="N">Alkylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001923" MajorTopicYN="N">Brain Chemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015180" MajorTopicYN="N">Electrophoresis, Gel, Two-Dimensional</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="Y">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014508" MajorTopicYN="N">Urea</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000520" MajorTopicYN="N">alpha-Glucosidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Protein dimer</Keyword><Keyword MajorTopicYN="Y">Protein reduction</Keyword><Keyword MajorTopicYN="Y">Urea</Keyword><Keyword MajorTopicYN="Y">Western blotting</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>07</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>09</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>10</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>10</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>10</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30312619</ArticleId><ArticleId IdType="pii">S0003-2697(18)30673-0</ArticleId><ArticleId IdType="doi">10.1016/j.ab.2018.10.008</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Kumari, Meena" sort="Kumari, Meena" uniqKey="Kumari M" first="Meena" last="Kumari">Meena Kumari</name></noRegion><name sortKey="Anji, Antje" sort="Anji, Antje" uniqKey="Anji A" first="Antje" last="Anji">Antje Anji</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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