Article
Malfolded cytochrome P-450(M1) localized in unusual membrane structures of the endoplasmic reticulum in cultured animal cells.
Journal of biochemistry - 1 Aug 1995
Ishihara N, Yamashina S, Sakaguchi M, Mihara K, Omura T
Abstract excerpt
A conserved region containing three to five proline residues is present just behind the signal-anchor sequence in the amino terminal portion of most microsomal cytochrome P-450s. We have shown that the proline residues are crucial for correct folding in Schizosaccharomyces pombe cells by using mu...
Topics
- Amino Acid Sequence
- Animals
- Aryl Hydrocarbon Hydroxylases
- Base Sequence
- Cell Line
- Cytochrome P-450 Enzyme System
- Endoplasmic Reticulum
- Intracellular Membranes
- Microscopy, Electron
- Molecular Sequence Data
- Mutation
- Oligodeoxyribonucleotides
- Protein Folding
- Steroid 16-alpha-Hydroxylase
- Steroid Hydroxylases
- Subcellular Fractions