Open AccessThe primary structure of artemin from Artemia cysts
Author(s) -
GRAAF Jack,
AMONS Reinout,
MÖLLER Wim
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19394.x
Subject(s) - edman degradation , protein primary structure , amino acid , biochemistry , histidine , biology , peptide sequence , amino acid analysis , chemistry , botany , gene
The primary structure of artemin, a major protein isolated from Artemia cysts, has been determined by direct Edman degradation of the purified protein. The amino‐terminal acetylated protein has 229 amino acid residues and a high content of histidine and cysteine/cystine. A search in the GenBank Data Base at Los Alamos, using the FASTA program [Pearson, W. R. & Lipman, D. J. (1988) Proc. Natl Acad. Sci. USA 85 , 2444–2448] revealed a limited but unmistakable similarity to ferritin from vertebrates.