Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase
Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein...
Ausführliche Beschreibung
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Englisch |
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1980 |
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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, 95(1980), 2, Seite 569-576 |
Übergeordnetes Werk: |
volume:95 ; year:1980 ; number:2 ; pages:569-576 |
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520 | |a Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. | ||
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(DE-627)NLEJ183555392 (DE-599)GBVNLZ183555392 DE-627 ger DE-627 rakwb eng Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Morgan, D.G. oth Routtenberg, A. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 2, Seite 569-576 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:2 pages:569-576 http://dx.doi.org/10.1016/0006-291X(80)90822-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 2 569-576 |
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(DE-627)NLEJ183555392 (DE-599)GBVNLZ183555392 DE-627 ger DE-627 rakwb eng Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Morgan, D.G. oth Routtenberg, A. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 2, Seite 569-576 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:2 pages:569-576 http://dx.doi.org/10.1016/0006-291X(80)90822-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 2 569-576 |
allfields_unstemmed |
(DE-627)NLEJ183555392 (DE-599)GBVNLZ183555392 DE-627 ger DE-627 rakwb eng Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Morgan, D.G. oth Routtenberg, A. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 2, Seite 569-576 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:2 pages:569-576 http://dx.doi.org/10.1016/0006-291X(80)90822-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 2 569-576 |
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(DE-627)NLEJ183555392 (DE-599)GBVNLZ183555392 DE-627 ger DE-627 rakwb eng Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Morgan, D.G. oth Routtenberg, A. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 2, Seite 569-576 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:2 pages:569-576 http://dx.doi.org/10.1016/0006-291X(80)90822-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 2 569-576 |
allfieldsSound |
(DE-627)NLEJ183555392 (DE-599)GBVNLZ183555392 DE-627 ger DE-627 rakwb eng Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Morgan, D.G. oth Routtenberg, A. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 2, Seite 569-576 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:2 pages:569-576 http://dx.doi.org/10.1016/0006-291X(80)90822-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 2 569-576 |
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evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase |
title_auth |
Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase |
abstract |
Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. |
abstractGer |
Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. |
abstract_unstemmed |
Phosphorylation of a brain protein of M"r=41,000, termed band F"2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F"2 on polyacrylamide gels and both appear as a doublet band of M"r=41,000-42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F"2 is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F"2 can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function. |
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