Amino-terminal sequence of phenobarbital-inducible cytochrome P-450 from rabbit liver microsomes: Similarity to hydrophobic amino-terminal segments of preproteins

SummaryThe amino-terminal sequence of two electrophoretically homogeneous forms of rabbit liver microsomal cytochrome P-450, P-450LM2 and P-45LM4, has been examined by automated Edman degradation. Methionine is the amino terminus of P-450LM2, and 17 of the first 20 residues are hydrophobic, including two clusters of five consecutive leucines. The composition and sequence of this region are similar to those of the short-lived hydrophobic amino-terminal precursor segments of certain other proteins, especially myeloma immunoglobulin light chains and pancreatic zymogens. Multiple amino-terminal residues, including methionine, were detected for P-450LM4 suggesting the presence of several highly similar forms of P-450 or that partial proteolysis had occurred.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/22857/1/0000419.pd

Terminal sequences of lysosome solubilized pig liver cytochrome b5 reductase

SummaryLysosome solubilized pig liver cytochrome b5 reductase has the following twenty residues as NH2-terminal sequence: Ser-Thr-Pro-Ala-Ile-Thr-Leu-Glu-Asn-Pro-Asp-Ile-Lys-Tyr-Pro-Leu-Arg-Leu-Ile-Asp. The fragment is predicted to exist largely in the random conformation with 2 [beta]-bends at residues 9-12 and 14-17. The reductase fragment appears clean enough for complete sequence investigation and is very similar to cathepsin D-solubilized rabbit liver cytochrome b5 reductase.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/23164/1/0000089.pd