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BioqfnPhetic tizreonine deaminase {Cthreonine hydr&mse deaminating, EC 4.2. I .I 6) is the first en--zyxrie Zn the patbway of isoleucine biosynthesis and is subject. to feedback itahibitian I$ this amino acid.The efkt ofisoleucine is reversed by v&m:. Threc~ nine deaminase has been purified frcm S&~ZO~~~~LJZ ~~~~inrzsniarn and some other microorganisms II-31 . Attempts to purify the enzyme from E. CC& wereha&p&red by the instability of the enzyme [4j.We made an attempt to purify threonine deaminrtse ofE_ c&i by means of affinity chromatography. The allosteric effecters isoleucine and vahne and the substrate threonine, respectively, were coupled to Sepharose [SJ and tested for their ability to remove thrconine deaminax from protek solutions-keucine as a structuid analowe of isoleucine and &c&e which does not interact specifically with threonine deaminase were included in this study.Of the amino acids tested, isoleucine bound to %pharose showed the strongest affinity for threonine

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