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PMID: 670203 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The primary structure of the nonpolar segment of bovine cytochrome b5.

The Journal of biological chemistry ·Vol. 253 ·No. 15 ·1978-08-10 ·Pages 5369-72

Fleming PJ, Dailey HA, Corcoran D, Strittmatter P

Abstract

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.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Cattle Circular Dichroism Cytochromes Male Microsomes, Liver/enzymology Peptide Fragments/analysis Protein Conformation
Chemicals
Amino Acids Cytochromes Peptide Fragments
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Fleming P J
Dailey H A
Corcoran D
Strittmatter P
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1978-08-10
Pages
5369-72
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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