Primary structure of cytochrome c from the Emu, Dromaeus novaehollandiae

Augusteyn R.C. (1973) Primary structure of cytochrome c from the Emu, Dromaeus novaehollandiae. BBA - Protein Structure, 303 1: 1-7. doi:10.1016/0005-2795(73)90141-4


Author Augusteyn R.C.
Title Primary structure of cytochrome c from the Emu, Dromaeus novaehollandiae
Journal name BBA - Protein Structure
ISSN 0005-2795
Publication date 1973-03-23
Sub-type Article (original research)
DOI 10.1016/0005-2795(73)90141-4
Volume 303
Issue 1
Start page 1
End page 7
Total pages 7
Subject 2700 Medicine
Abstract Twenty peptides, including the haemopeptide, were isolated from a limited chymotryptic digest of cytochrome c from the skeletal muscle of the emu by chromatography on Whatman phosphocellulose P-70. These peptides were purified by electrophoresis or chromatography on paper and their sequences were determined. The complete sequence of the protein was deduced by alignment of these peptides with the known sequences of several other cytochromes c. Emu cytochrome c differs from the chicken protein in 2 positions. The most interesting feature of the sequence is the substitution of asparagine for the histidine residue found in position 33 of most other cytochromes c.
Q-Index Code C1
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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