Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.
Identifieur interne : 000512 ( Main/Curation ); précédent : 000511; suivant : 000513Evaluation 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
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pubmed:1379250Le document en format XML
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<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>
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<author><name sortKey="Sulkowski, E" sort="Sulkowski, E" uniqKey="Sulkowski E" first="E" last="Sulkowski">E. Sulkowski</name>
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<author><name sortKey="Andersson, L" sort="Andersson, L" uniqKey="Andersson L" first="L" last="Andersson">L. Andersson</name>
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<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>
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<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>
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<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1379250</PMID>
<DateCompleted><Year>1992</Year>
<Month>09</Month>
<Day>03</Day>
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<DateRevised><Year>2019</Year>
<Month>06</Month>
<Day>29</Day>
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<Issue>1</Issue>
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<Month>Jun</Month>
<Day>26</Day>
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<Title>Journal of chromatography</Title>
<ISOAbbreviation>J Chromatogr</ISOAbbreviation>
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<ArticleTitle>Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.</ArticleTitle>
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<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>
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