Phosphorylation of microsome-bound cytochrome P-450 LM2 |
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Authors: | W Pyerin M Marx H Taniguchi |
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Affiliation: | Institute of Experimental Pathology, German Cancer Research Center, Im Neuenheimer Feld 280, D-6900 Heidelberg, FRG |
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Abstract: | The phosphorylation of a microsomal protein of rabbit liver by catalytic subunit of cyclic AMP-dependent protein kinase was shown, and the protein was identified as cytochrome P-450 LM2 on basis of comparative peptide-mapping. Acid hydrolysis of microsome-bound phosphorylated cytochrome P-450 revealed that phosphorylation occurred exclusively on serine residues. This serine residue was identified as the same residue phosphorylated in purified, soluble P-450, that is, serine in position 128. |
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