Presence of a prepiece at the NH2-terminal end of pre-cytochrome P-450(SCC) peptide.
Mild acid treatment of in vitro translated cytochrome P-450(SCC) (pre-P-450(SCC] peptide cleaved the peptide into two fragments. Comparison of the sizes and the NH2-terminal amino acids of the fragments with those of the corresponding fragments from mature P-450(SCC) suggested that the prepiece of pre-P-450(SCC) was present at the NH2-terminal end of the peptide. This conclusion was confirmed by radio-sequencing of the NH2-terminal portion of pre-P-450(SCC).
D000302:Adrenal Cortex / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D008928:Mitochondria / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D014176:Protein Biosynthesis; D012313:RNA / Q000235:genetics; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism
D010446:Peptide Fragments; D012313:RNA; D003577:Cytochrome P-450 Enzyme System