Purification of the cAMP receptor protein by affinity chromatography
References (22)
- et al.
Biochem. Biophys. Res. Commun.
(1970) - et al.
Biochem. Biophys. Res. Commun.
(1970) - et al.
Biochem. Biophys. Res. Commun.
(1971) - et al.
J. Biol. Chem.
(1971) - et al.
J. Biol. Chem.
(1972) - et al.
J. Biol. Chem.
(1971) - et al.
J. Biol. Chem.
(1973) - et al.
J. Biol. Chem.
(1973) J. Biol. Chem.
(1970)- et al.
J. Biol. Chem.
(1968)
J. Biol. Chem.
(1951)
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Structural diversity of the cAMP-dependent protein kinase regulatory subunit in Caenorhabditis elegans
2013, Cellular SignallingCitation Excerpt :The latter two fractions were combined for analysis. The presence of urea was necessitated by the relatively high affinity of R-subunits for cAMP [18]. As shown in Table 4, using this treatment, a number of candidate polypeptides were eluted in the expected molecular weight range (35–43 kDa) for the R-subunit isoforms predicted to occur in C. elegans.
Isolation of the myc transcription factor nucleoside diphosphate kinase and the multifunctional enzyme glyceraldehyde-3-phosphate dehydrogenase by cAMP affinity chromatography
1995, International Journal of Biochemistry and Cell BiologyCyclic Nucleotide-Dependent Protein Kinases
1986, EnzymesThe synthesis and characterisation of a cyclic AMP-sepharose 4B matrix with affinity for cyclic AMP-dependent proteins
1980, Journal of Biochemical and Biophysical Methods
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