The primary structure of the nonpolar segment of bovine cytochrome b5

The primary structure of the membrane bound segment of amphipathic bovine liver microsomal cytochrome b5 has been determined. This 43 residue nonpolar polypeptide is present at the COOH terminus of cytochrome b5. The sequence was obtained by automated sequence analysis and carboxypeptidase digestion...

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Veröffentlicht in:	The Journal of biological chemistry 1978-08, Vol.253 (15), p.5369-5372
Hauptverfasser:	Fleming, P J, Dailey, H A, Corcoran, D, Strittmatter, P
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - analysis Animals Cattle Circular Dichroism Cytochromes Male Microsomes, Liver - enzymology Peptide Fragments - analysis Protein Conformation
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Zusammenfassung:	The primary structure of the membrane bound segment of amphipathic bovine liver microsomal cytochrome b5 has been determined. This 43 residue nonpolar polypeptide is present at the COOH terminus of cytochrome b5. The sequence was obtained by automated sequence analysis and carboxypeptidase digestions. The sequence obtained is: Ile-Thr-Lys-Pro-Ser-Glu-Ser-Ile-Ile-Thr-Ile-Asp-Ser-Asn-Pro-Ser-Trp-Trp-Thr-Asn-Trp-Leu-Ile-Pro-Ala-Ile-Ser-Ala-Leu-Phe-Val-Ala-Leu-Ile-Tyr-His-Leu-Tyr-Thr-Ser-Glu-Asn. Conformational analysis using predictive algorithms is presented along with circular dichroism data on the peptide bound to phospholipid vesicles.
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(17)30380-0