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Primary structure of myohemerythrin from the annelid Nereis diversicolor
Author(s) -
Takagi Takashi,
Cox Jos.A.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80716-g
Subject(s) - subfamily , trichloroacetic acid , protein primary structure , chemistry , peptide sequence , cysteine , amino acid , homology (biology) , biochemistry , biology , stereochemistry , gene , enzyme
The metal‐free form of Nereis diversicolor myohemerythrin was purified from whole animal extracts by trichloroacetic acid precipitation and ion exchange chromatography. The amino acid sequence of myohemerythrin has been determined. The protein is composed of 120 residues, possesses an unblocked N‐terminus and is devoid of cysteine residues. It bears 62% sequence identity with Themiste zostericola myohemerythrin, the only other member of this subfamily sequenced to date. Within the family of hemerythrins, homology is particularly high in the segments involved in the binding of the two iron atoms and in the β‐turn‐rich N‐terminal segment.