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Heterogeneity of adrenocortical ferredoxin
Author(s) -
Hiwatashi Atsuo,
Sakihama Naoko,
Shin Masateru,
Ichikawa Yoshiyuki
Publication year - 1986
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(86)81133-4
Subject(s) - ferredoxin , chemistry , chromatography , amino acid , alanine , homogeneous , glycine , serine , biochemistry , cytochrome , enzyme , physics , thermodynamics
Bovine adrenocortical ferredoxin (adreno‐ferredoxin) was purified from adrenocortical mitochondria by an improved method that included hydrophobic chromatography on Toyopearl gels. The purified ferredoxin was electrophoretically homogeneous. It was further separated into five fractions by hydrophobic chromatography on a TSK‐gel phenyl‐5PW column with a high‐pressure liquid chromatography system. The properties of the three main fractions were examined. The fractions had identical absorption spectra and almost the same activity in an NADPH‐cytochrome c reducing system. Their amino‐terminal sequences all corresponded to the reported sequence, but the carboxyl‐terminal residues were glycine or serine, not alanine as reported. These results indicate that these adreno‐ferredoxins had additional amino acid residues at the carboxyl end. It seems that adreno‐ferredoxin extracted from mitochondria undergoes proteolytic attack during purification to become heterogeneous.