Reference: SEAMAN GR (1959) Purification of an enzyme from yeast which liberates protein-bound thioctic acid. J Biol Chem 234(1):161-4

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Abstract


Removal of thioctic acid from enzyme proteins may be accomplished by treatment of crude tissue or cell extracts with adsorption alumina (1). This procedure lowers the thioctic acid content of alpha-keto acid oxidases in cell-free extracts of Tetrahymena (2). King et al. (3) have also used the procedure to reduce the thioctic acid content of extracts of Acetobacter suboxydans. The effectiveness of the procedure is dependent (4) upon the presence in crude extracts of an enzyme which releases protein-bound thioctic acid; the liberated cofactor is then adsorbed on the alumina. Crude preparations of this enzyme have been obtained by a single ammonium sulfate fractionation of pigeon liver acetone powder (1, 4). Reed (5) recently reported a "lipoyl-x hydrolase" in Streptococcus faecalis; this is apparently the enzyme responsible for that decrease in thioctic acid content of crude extracts of this organism which is achieved by alumina treatment (1). The present report describes a procedure for purification of an enzyme from baker's yeast which liberates protein-bound thioctic acid.

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