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.
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| rdfs:comment |
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.
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| uniprot:name |
J. Biochem.
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| uniprot:author |
Kominami S.,
Ogishima T.,
Okada Y.,
Omura T.,
Takemori S.
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| uniprot:date |
1983
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| uniprot:pages |
1711-1714
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| uniprot:title |
Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex.
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| uniprot:volume |
94
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