| Autor: |
Thurmond, Jennifer M., Hards, Robert G., Seipelt, C.Thomas, Leonard, Amanda E., Hansson, Lennart, Strömqvist, Mats, Byström, Mona, Enquist, Kerstin, Xu, Bixiong C., Kopchick, John J., Mukerji, Pradip |
| Zdroj: |
Protein Expression and Purification; July 1997, Vol. 10 Issue: 2 p202-208, 7p |
| Abstrakt: |
Specific serine and threonine residues of recombinant human β-casein produced inEscherichia coliwere shown to be phosphorylatedin vivowhen human casein kinase II was coexpressed in the same plasmid. All of the phosphorylated forms found in the native protein were also detected in the recombinant protein. The phosphorylation of recombinant human β-casein was confirmed by immunoblots, fast protein liquid chromatography, urea–polyacrylamide gel electrophoresis, SDS–polyacrylamide gel electrophoresis, and liquid chromatography–mass spectrometry. The results indicate that the substrate specificity of casein kinase IIin vivowas unaffected in its recombinant form. This is the first demonstration ofin vivophosphorylation of specific residues of a multiphosphorylated protein produced inE. coliwith a single plasmid. |
| Databáze: |
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| Externí odkaz: |
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