Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex.
Partial amino acid sequences of two mitochondrial cytochrome P-450's, P-450 (SCC) and P-450 (11 beta), and two microsomal cytochrome P-450's, P-450 (C-21), and P-450 (17 alpha, Lyase), from adrenal cortex were analyzed and compared. Mitochondrial P-450's and microsomal P-450's were different in the amino acid sequences at their NH2-terminals. The sequences of microsomal P-450's started from terminal methionine and were highly hydrophobic, whereas those of mitochondrial P-450's lacked NH2-terminal methionine and were not hydrophobic. These findings strongly suggest that the NH2-terminal portions of newly synthesized P-450's determine their intracellular localization to different cell organelles.
D000302:Adrenal Cortex / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008861:Microsomes / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology*
D003577:Cytochrome P-450 Enzyme System