A new method of purification of rat liver L-threonine deaminase has been developed, and the results obtained are compared with values obtained by other authors. Some properties of this enzyme (pH optimum, temperature optimum, thermal stability, specificity, etc.) have been examined and we found that the enzyme is inhibited by carbonate ions, that L-cysteine (a competitive inhibitor) is also an inactivator of the enzyme and that it is bound to the enzyme in a ratio of 0.25 mole of cysteine per mole of enzyme, supporting the hypothesis that the enzyme consists of 4 subunits. © 1985 The Nobel Foundation.
Leoncini, R., Pagani, R., Casella, A., Marinello, E. (1985). Rat Liver L-Threonine Deaminase Properties and Purification. BIOSCIENCE REPORTS, 5(6), 499-508 [10.1007/BF01116949].
Rat Liver L-Threonine Deaminase Properties and Purification
Leoncini, R.;Pagani, R.;Marinello, E.
1985-01-01
Abstract
A new method of purification of rat liver L-threonine deaminase has been developed, and the results obtained are compared with values obtained by other authors. Some properties of this enzyme (pH optimum, temperature optimum, thermal stability, specificity, etc.) have been examined and we found that the enzyme is inhibited by carbonate ions, that L-cysteine (a competitive inhibitor) is also an inactivator of the enzyme and that it is bound to the enzyme in a ratio of 0.25 mole of cysteine per mole of enzyme, supporting the hypothesis that the enzyme consists of 4 subunits. © 1985 The Nobel Foundation.
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https://hdl.handle.net/11365/28890
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