The covalent structure of rabbit phenobarbital-induced cytochrome P-450. Partial amino acid sequence and order of cyanogen bromide peptides.
Open Access
- 1 December 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (24) , 14988-14999
- https://doi.org/10.1016/s0021-9258(18)33382-9
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Primary structure of a cytochrome P-450: coding nucleotide sequence of phenobarbital-inducible cytochrome P-450 cDNA from rat liver.Proceedings of the National Academy of Sciences, 1982
- The primary structure of the monoxygenase cytochrome P450CAMBiochemical and Biophysical Research Communications, 1982
- The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesisCell, 1981
- Oxygen Activation by Cytochrome P-4501Annual Review of Biochemistry, 1980
- Polyquarternary amines prevent peptide loss from sequenatorsAnalytical Biochemistry, 1978
- Amino-terminal sequence of phenobarbital-inducible cytochrome P-450 from rabbit liver microsomes: Similarity to hydrophobic amino-terminal segments of preproteinsBiochemical and Biophysical Research Communications, 1977
- The structure of intrinsic membrane proteinsJournal of Supramolecular Structure, 1977
- Structural aspects of the membrane of the endoplasmic reticulumBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1975
- The Effect of Neighboring Charges on the Helix Forming Ability of Charged Amino Acids in ProteinsMacromolecules, 1975
- Molecular structure determination by electron microscopy of unstained crystalline specimensJournal of Molecular Biology, 1975