Isolation of the myc transcription factor nucleoside diphosphate kinase and the multifunctional enzyme glyceraldehyde-3-phosphate dehydrogenase by cAMP affinity chromatography.
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Isolation of the myc transcription factor nucleoside diphosphate kinase and the multifunctional enzyme glyceraldehyde-3-phosphate dehydrogenase by cAMP affinity chromatography. / Weber, B; Weber, Wolfgang; Buck, F; Hilz, H.
in: INT J BIOCHEM CELL B, Jahrgang 27, Nr. 2, 2, 1995, S. 215-224.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Isolation of the myc transcription factor nucleoside diphosphate kinase and the multifunctional enzyme glyceraldehyde-3-phosphate dehydrogenase by cAMP affinity chromatography.
AU - Weber, B
AU - Weber, Wolfgang
AU - Buck, F
AU - Hilz, H
PY - 1995
Y1 - 1995
N2 - Cyclic AMP affinity chromatography applied to various mammalian tissue extracts yielded two proteins in addition to the regulatory subunits of protein kinase. This paper characterizes these proteins and provides a simple procedure for their preparation. The polypeptides (36 kDa and a 19 kDa/21 kDa doublet) were isolated from the cAMP matrix by sequential elution with cAMP solutions of increasing concentrations. Microsequencing was accomplished following chemical or enzymic degradation of isolated polypeptides. Partial amino acid sequences of the 36 kDa protein and analyses of its enzymic activity indicated identity with glyceraldehyde-3-phosphate dehydrogenase whilst the lower MW protein proved to be identical with mammalian nucleoside diphosphate kinase subunits. In both cases, binding to cAMP appeared to occur at the nucleotide (NAD and ATP, respectively) sites. In conclusion, we present a one step-procedure, applicable to tissue and cell extracts, which allows the simultaneous isolation of both glyceraldehyde-3-phosphate dehydrogenase and nucleoside diphosphate kinase. This procedure may help to elucidate the multiple functions of these two important enzymes.
AB - Cyclic AMP affinity chromatography applied to various mammalian tissue extracts yielded two proteins in addition to the regulatory subunits of protein kinase. This paper characterizes these proteins and provides a simple procedure for their preparation. The polypeptides (36 kDa and a 19 kDa/21 kDa doublet) were isolated from the cAMP matrix by sequential elution with cAMP solutions of increasing concentrations. Microsequencing was accomplished following chemical or enzymic degradation of isolated polypeptides. Partial amino acid sequences of the 36 kDa protein and analyses of its enzymic activity indicated identity with glyceraldehyde-3-phosphate dehydrogenase whilst the lower MW protein proved to be identical with mammalian nucleoside diphosphate kinase subunits. In both cases, binding to cAMP appeared to occur at the nucleotide (NAD and ATP, respectively) sites. In conclusion, we present a one step-procedure, applicable to tissue and cell extracts, which allows the simultaneous isolation of both glyceraldehyde-3-phosphate dehydrogenase and nucleoside diphosphate kinase. This procedure may help to elucidate the multiple functions of these two important enzymes.
KW - Animals
KW - Humans
KW - Rats
KW - Rabbits
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Sequence Homology, Amino Acid
KW - Hela Cells
KW - Molecular Weight
KW - Chromatography, Affinity
KW - Cyclic AMP
KW - Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/isolation & purification/metabolism
KW - Muscle, Skeletal/enzymology
KW - Nucleoside-Diphosphate Kinase/chemistry/isolation & purification/metabolism
KW - Peptide Fragments/chemistry/isolation & purification
KW - Proto-Oncogene Proteins c-myc/chemistry/isolation & purification
KW - Saccharomyces cerevisiae/enzymology
KW - Transcription Factors/chemistry/isolation & purification
KW - Animals
KW - Humans
KW - Rats
KW - Rabbits
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Sequence Homology, Amino Acid
KW - Hela Cells
KW - Molecular Weight
KW - Chromatography, Affinity
KW - Cyclic AMP
KW - Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/isolation & purification/metabolism
KW - Muscle, Skeletal/enzymology
KW - Nucleoside-Diphosphate Kinase/chemistry/isolation & purification/metabolism
KW - Peptide Fragments/chemistry/isolation & purification
KW - Proto-Oncogene Proteins c-myc/chemistry/isolation & purification
KW - Saccharomyces cerevisiae/enzymology
KW - Transcription Factors/chemistry/isolation & purification
M3 - SCORING: Journal article
VL - 27
SP - 215
EP - 224
JO - INT J BIOCHEM CELL B
JF - INT J BIOCHEM CELL B
SN - 1357-2725
IS - 2
M1 - 2
ER -
