The amino acid sequence of cytochrome f from the brown alga Alaria esculenta (L.) Grev.
Cytochrome f was isolated from the brown alga Alaria esculenta and the amino acid sequence was determined. The native haemoprotein has a molecular weight of 9800 and consists of a single polypeptide chain of 86 amino acid residues with a haem group bonded to cysteine residues at positions 14 and 17. The N-terminus is not acetylated and no methylated lysines were found. Sequences of three other algal cytochromes f were compared with that of Alaria and 22 out of 92 positions were common to the four sequences. One-half of these conserved sites occur between positions 49 and 63. Detailed evidence for the amino acid sequence of Alaria cytochrome has been deposited as Supplementary Publication SUP 50048 (6 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975) 145, 5.
D000595:Amino Acid Sequence; D003580:Cytochromes / Q000032:analysis; D004150:Dipeptidases; D056890:Eukaryota / Q000032:analysis*; D006418:Heme / Q000032:analysis; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D000459:Phaeophyceae / Q000032:analysis*; D013045:Species Specificity; D014357:Trypsin
D003580:Cytochromes; D010446:Peptide Fragments; D006418:Heme; D004150:Dipeptidases; D014357:Trypsin