Primary structure of the membranous segment of cytochrome b5.
AUTOR(ES)
Ozols, J
RESUMO
The primary structure of the membranous segment of porcine liver microsomal cytochrome b5 has been determined. This polypeptide is at the COOH terminus of the cytochrome molecule and consists of 43 amino acids. It is essential for the insertion of the cytochrome into the endoplasmic reticular membrane. Automated sequence analysis of tryptic and cyanogen bromide/anhydrous heptafluorobutyric acid peptides provided data from which the following unique amino acid sequence was deduced: Ile-Ala-Lys-Pro-Ser-Glu-Thr-Leu-Ile-Thr-Thr-Val-Glu-Ser-Asn-Ser-Ser-Trp-Trp-Thr-Asn-Trp-Val-Ile-Pro-Ala-Ile-Ser-Ala-Leu-Val-Val-Ser-Leu-Met-Tyr-His-Phe-Tyr-Thr-Ser-Glu-Asn. A prediction of alpha-helices, beta-structures, and beta-turns basedon the sequence of this polypeptide is also presented.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=431705Documentos Relacionados
- Evidence that two forms of bovine erythrocyte cytochrome b5 are identical to segments of microsomal cytochrome b5.
- Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5.
- Comparative Study of the Primary Structures of Cytochrome b5 from Four Species*
- Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b.
- PRIMARY STRUCTURE AND EVOLUTION OF CYTOCHROME C