Preparation and properties of clostridial ferredoxins.
作者： Jesse Rabinowitz
DOI: 10.1016/0076-6879(72)24089-7
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摘要: Publisher Summary This chapter discusses the preparation and properties of Clostridial Ferredoxins. Ferredoxin was first isolated from Clostridium pasteurianum . The protein functions as an electron transfer factor in enzymatic formation acetyl phosphate hydrogen pyruvate by extracts that organism treated with diethylaminoethyl (DEAE)-cellulose a variety other reactions described. It is characterized iron–sulfur when presence acid-labile sulfur recognized. found all clostridial species are examined. Procedures for purification ferredoxin based on acidic nature its resultant high affinity DEAE-cellulose, small size relative to proteins solubility acetone, ease crystallization ammonium sulfate. has molecular weight about 6000 composed single polypeptide chain containing 55 or fewer amino acid residues, 8 which cysteine. biological activity this associated unusually low redox potential.
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