Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.
Identifieur interne : 000516 ( Main/Exploration ); précédent : 000515; suivant : 000517Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.
Auteurs : L. Andersson [Suède] ; E. SulkowskiSource :
- Journal of chromatography ; 1992.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Aprotinine (composition chimique), Bovins (MeSH), Canards (MeSH), Cations divalents (MeSH), Chromatographie d'affinité (méthodes), Concentration en ions d'hydrogène (MeSH), Cuivre (composition chimique), Données de séquences moléculaires (MeSH), Liaison aux protéines (MeSH), Lysozyme (composition chimique), Métaux (composition chimique), Nickel (composition chimique), Protéines (composition chimique), Protéines végétales (composition chimique), Spectrophotométrie UV (MeSH), Séquence d'acides aminés (MeSH), Zinc (composition chimique), Édulcorants (MeSH).
- MESH :
- composition chimique : Aprotinine, Cuivre, Lysozyme, Métaux, Nickel, Protéines, Protéines végétales, Zinc.
- méthodes : Chromatographie d'affinité.
- Animaux, Bovins, Canards, Cations divalents, Concentration en ions d'hydrogène, Données de séquences moléculaires, Liaison aux protéines, Spectrophotométrie UV, Séquence d'acides aminés, Édulcorants.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Aprotinin (chemistry), Cations, Divalent (MeSH), Cattle (MeSH), Chromatography, Affinity (methods), Copper (chemistry), Ducks (MeSH), Hydrogen-Ion Concentration (MeSH), Metals (chemistry), Molecular Sequence Data (MeSH), Muramidase (chemistry), Nickel (chemistry), Plant Proteins (chemistry), Protein Binding (MeSH), Proteins (chemistry), Spectrophotometry, Ultraviolet (MeSH), Sweetening Agents (MeSH), Zinc (chemistry).
- MESH :
- chemical , chemistry : Aprotinin, Copper, Metals, Muramidase, Nickel, Plant Proteins, Proteins, Zinc.
- methods : Chromatography, Affinity.
- Amino Acid Sequence, Animals, Cations, Divalent, Cattle, Ducks, Hydrogen-Ion Concentration, Molecular Sequence Data, Protein Binding, Spectrophotometry, Ultraviolet, Sweetening Agents.
Abstract
The adsorption properties of various peptides and proteins, lacking histidyl groups, on immobilized Cu(II), Ni(II), Zn(II) and Co(II) ions are described; at pH 6 and below they were little retarded. At higher pH the retention became pronounced for iminodiacetate (IDA)-Cu(II) gel. This effect seems to be related to the presence of a terminal alpha-amino group; in the absence of this group the retention of the protein was largely eliminated. At pH 8.5 a terminal alpha-amino group is adsorbed as strongly as a histidyl group. IDA-Ni(II), IDA-Zn(II) and IDA-Co(II) gels display little or no attraction for the terminal alpha-amino group of a protein.
DOI: 10.1016/0021-9673(92)85523-v
PubMed: 1379250
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Sulkowski</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1992">1992</date><idno type="RBID">pubmed:1379250</idno><idno type="pmid">1379250</idno><idno type="doi">10.1016/0021-9673(92)85523-v</idno><idno type="wicri:Area/Main/Corpus">000512</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000512</idno><idno type="wicri:Area/Main/Curation">000512</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000512</idno><idno type="wicri:Area/Main/Exploration">000512</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.</title><author><name sortKey="Andersson, L" sort="Andersson, L" uniqKey="Andersson L" first="L" last="Andersson">L. Andersson</name><affiliation wicri:level="1"><nlm:affiliation>Biochemical Separation Centre, University of Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Biochemical Separation Centre, University of Uppsala</wicri:regionArea><wicri:noRegion>University of Uppsala</wicri:noRegion></affiliation></author><author><name sortKey="Sulkowski, E" sort="Sulkowski, E" uniqKey="Sulkowski E" first="E" last="Sulkowski">E. Sulkowski</name></author></analytic><series><title level="j">Journal of chromatography</title><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Aprotinin (chemistry)</term><term>Cations, Divalent (MeSH)</term><term>Cattle (MeSH)</term><term>Chromatography, Affinity (methods)</term><term>Copper (chemistry)</term><term>Ducks (MeSH)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Metals (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Muramidase (chemistry)</term><term>Nickel (chemistry)</term><term>Plant Proteins (chemistry)</term><term>Protein Binding (MeSH)</term><term>Proteins (chemistry)</term><term>Spectrophotometry, Ultraviolet (MeSH)</term><term>Sweetening Agents (MeSH)</term><term>Zinc (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Aprotinine (composition chimique)</term><term>Bovins (MeSH)</term><term>Canards (MeSH)</term><term>Cations divalents (MeSH)</term><term>Chromatographie d'affinité (méthodes)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Cuivre (composition chimique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Lysozyme (composition chimique)</term><term>Métaux (composition chimique)</term><term>Nickel (composition chimique)</term><term>Protéines (composition chimique)</term><term>Protéines végétales (composition chimique)</term><term>Spectrophotométrie UV (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Zinc (composition chimique)</term><term>Édulcorants (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aprotinin</term><term>Copper</term><term>Metals</term><term>Muramidase</term><term>Nickel</term><term>Plant Proteins</term><term>Proteins</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Aprotinine</term><term>Cuivre</term><term>Lysozyme</term><term>Métaux</term><term>Nickel</term><term>Protéines</term><term>Protéines végétales</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chromatography, Affinity</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Chromatographie d'affinité</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cations, Divalent</term><term>Cattle</term><term>Ducks</term><term>Hydrogen-Ion Concentration</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Spectrophotometry, Ultraviolet</term><term>Sweetening Agents</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Canards</term><term>Cations divalents</term><term>Concentration en ions d'hydrogène</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Spectrophotométrie UV</term><term>Séquence d'acides aminés</term><term>Édulcorants</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The adsorption properties of various peptides and proteins, lacking histidyl groups, on immobilized Cu(II), Ni(II), Zn(II) and Co(II) ions are described; at pH 6 and below they were little retarded. At higher pH the retention became pronounced for iminodiacetate (IDA)-Cu(II) gel. This effect seems to be related to the presence of a terminal alpha-amino group; in the absence of this group the retention of the protein was largely eliminated. At pH 8.5 a terminal alpha-amino group is adsorbed as strongly as a histidyl group. IDA-Ni(II), IDA-Zn(II) and IDA-Co(II) gels display little or no attraction for the terminal alpha-amino group of a protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1379250</PMID><DateCompleted><Year>1992</Year><Month>09</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>29</Day></DateRevised><Article PubModel="Print"><Journal><JournalIssue CitedMedium="Print"><Volume>604</Volume><Issue>1</Issue><PubDate><Year>1992</Year><Month>Jun</Month><Day>26</Day></PubDate></JournalIssue><Title>Journal of chromatography</Title><ISOAbbreviation>J Chromatogr</ISOAbbreviation></Journal><ArticleTitle>Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.</ArticleTitle><Pagination><MedlinePgn>13-7</MedlinePgn></Pagination><Abstract><AbstractText>The adsorption properties of various peptides and proteins, lacking histidyl groups, on immobilized Cu(II), Ni(II), Zn(II) and Co(II) ions are described; at pH 6 and below they were little retarded. At higher pH the retention became pronounced for iminodiacetate (IDA)-Cu(II) gel. This effect seems to be related to the presence of a terminal alpha-amino group; in the absence of this group the retention of the protein was largely eliminated. At pH 8.5 a terminal alpha-amino group is adsorbed as strongly as a histidyl group. IDA-Ni(II), IDA-Zn(II) and IDA-Co(II) gels display little or no attraction for the terminal alpha-amino group of a protein.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Andersson</LastName><ForeName>L</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Biochemical Separation Centre, University of Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sulkowski</LastName><ForeName>E</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Chromatogr</MedlineTA><NlmUniqueID>0427043</NlmUniqueID></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002413">Cations, Divalent</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008670">Metals</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013549">Sweetening Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>7OV03QG267</RegistryNumber><NameOfSubstance UI="D009532">Nickel</NameOfSubstance></Chemical><Chemical><RegistryNumber>9087-70-1</RegistryNumber><NameOfSubstance UI="D007611">Aprotinin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.17</RegistryNumber><NameOfSubstance UI="D009113">Muramidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber><NameOfSubstance UI="D015032">Zinc</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007611" MajorTopicYN="N">Aprotinin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002413" MajorTopicYN="N">Cations, Divalent</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002846" MajorTopicYN="N">Chromatography, Affinity</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004372" MajorTopicYN="N">Ducks</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008670" MajorTopicYN="N">Metals</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009113" MajorTopicYN="N">Muramidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName 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MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>6</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>6</Month><Day>26</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>6</Month><Day>26</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1379250</ArticleId><ArticleId IdType="doi">10.1016/0021-9673(92)85523-v</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Sulkowski, E" sort="Sulkowski, E" uniqKey="Sulkowski E" first="E" last="Sulkowski">E. Sulkowski</name></noCountry><country name="Suède"><noRegion><name sortKey="Andersson, L" sort="Andersson, L" uniqKey="Andersson L" first="L" last="Andersson">L. Andersson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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