^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases
^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not...
Ausführliche Beschreibung
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Englisch |
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1970 |
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Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 39(1970), 4, Seite 707-711 |
Übergeordnetes Werk: |
volume:39 ; year:1970 ; number:4 ; pages:707-711 |
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(DE-627)NLEJ184209536 (DE-599)GBVNLZ184209536 DE-627 ger DE-627 rakwb eng ^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Fritz, K.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 39(1970), 4, Seite 707-711 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:39 year:1970 number:4 pages:707-711 http://dx.doi.org/10.1016/0006-291X(70)90262-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 39 1970 4 707-711 |
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(DE-627)NLEJ184209536 (DE-599)GBVNLZ184209536 DE-627 ger DE-627 rakwb eng ^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Fritz, K.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 39(1970), 4, Seite 707-711 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:39 year:1970 number:4 pages:707-711 http://dx.doi.org/10.1016/0006-291X(70)90262-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 39 1970 4 707-711 |
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(DE-627)NLEJ184209536 (DE-599)GBVNLZ184209536 DE-627 ger DE-627 rakwb eng ^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Fritz, K.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 39(1970), 4, Seite 707-711 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:39 year:1970 number:4 pages:707-711 http://dx.doi.org/10.1016/0006-291X(70)90262-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 39 1970 4 707-711 |
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(DE-627)NLEJ184209536 (DE-599)GBVNLZ184209536 DE-627 ger DE-627 rakwb eng ^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Fritz, K.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 39(1970), 4, Seite 707-711 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:39 year:1970 number:4 pages:707-711 http://dx.doi.org/10.1016/0006-291X(70)90262-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 39 1970 4 707-711 |
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(DE-627)NLEJ184209536 (DE-599)GBVNLZ184209536 DE-627 ger DE-627 rakwb eng ^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Fritz, K.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 39(1970), 4, Seite 707-711 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:39 year:1970 number:4 pages:707-711 http://dx.doi.org/10.1016/0006-291X(70)90262-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 39 1970 4 707-711 |
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^3^5cl-nmr studies of co^2^+ carbonic anhydrases |
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^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases |
abstract |
^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. |
abstractGer |
^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. |
abstract_unstemmed |
^3^5Cl NMR studies of Co^2^+ substituted carbonic anhydrase (CA) reveal a difference in the pK of hydrolysis for the high and low specific activity forms of the enzyme in agreement with studies on the zinc enzymes. A time dependence was observed for the reaction of Co^2^+ with bovine apo CA but not with human B apo CA. A CN^- titration of the Co^2^+ CA indicates only one cobalt-chloride binding site. This work indicates that ^3^5Cl NMR can be used to monitor the interaction of Co^2^+ ions with proteins. |
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^3^5Cl-NMR studies of Co^2^+ carbonic anhydrases |
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