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Direct expression in Escherichia coli and characterization of bovine adrenodoxins with modified amino‐terminal regions
Author(s) -
Sagara Yasuhiro,
Hara Takayuki,
Ariyasu Yasuyuki,
Ando Fumiko,
Tokunaga Naomi,
Horiuchi Tadao
Publication year - 1992
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(92)80847-a
Subject(s) - escherichia coli , terminal (telecommunication) , chemistry , escherichia coli proteins , biochemistry , microbiology and biotechnology , biology , gene , computer science , telecommunications
Four forms of bovine adrenodoxin with modified amino‐termini obtained by direct expression of cDNAs in Escherichia coli are Ad(Met 1 ), Ad(Met −1 ), Ad(Met −12 ), and Ad(Met 6 ). The shoulder numbers represent this site of translation initiator Met at the amino‐termini. The adrenodoxins, except for Ad(Met −1 ), were purified from the cell lysate and the ratios of A 414 ‐to‐ A 276 of the purified proteins were over 0.92. NADPH‐cytochrome c reductase activities of the three forms of adrenodoxin in the presence of adrenodoxin reductase were the same as that of purified bovine adrenocortical adrenodoxin. However, as cytochrome P ‐450 SCC reduction catalyzed by Ad(Met 0 ) was about 60% or that by Ad(Met 1 ), the contribution of the amino‐terminal region for the electron transfer or binding to cytochrome P ‐450 SCC would need to be considered.