Primary structure of the membrane-binding segment of rabbit cytochrome b5.
The primary structure of the membrane-binding segment of rabbit cytochrome b5 has been determined. This segment, prepared by trypsin digestion of the intact protein, consists of 43 amino acid residues and corresponds to the COOH-terminal end (residues 91-133) of the parent molecule. Deduction of the primary structure was based on automated sequence analysis of the whole segment as well as manual and dansyl-Edman degradations of peptide fragments produced by CNBr cleavage and partial acid hydrolysis. The sequence obtained is: Leu-Ser-Lys-Pro-Met-Glu-Thr-Leu-Ile-Thr-Thr-Val-Asn-Ser-Asn-Ser-Ser-Trp-Trp-Thr-Asn-Trp-Val-Ile-Pro-Ala-Ile-Ser-Ala-Leu-Ile-Val-Ala-Leu-Met-Tyr-Arg-Leu-Tyr-Met-Ala-Asp-Asp. This sequence is 63 to 81% homologous with respect to those determined for the membrane-binding segments of equine, porcine and bovine cytochrome b5. The interaction of this segment with phospholipid bilayer membranes is discussed, and a prediction of its secondary structure is also presented.
D000595:Amino Acid Sequence; D000818:Animals; D003488:Cyanogen Bromide; D003580:Cytochromes / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D011817:Rabbits
D003580:Cytochromes; D010446:Peptide Fragments; D003488:Cyanogen Bromide