A study of the purification and properties of tryptophan synthatase of bengal gram (Cicer arietinum)

Madhusudanan, P. ; Vaidyanathan, C. S. (1964) A study of the purification and properties of tryptophan synthatase of bengal gram (Cicer arietinum) Archives of Biochemistry and Biophysics, 104 (3). pp. 405-415. ISSN 0003-9861

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Official URL: http://www.sciencedirect.com/science/article/pii/0...

Related URL: http://dx.doi.org/10.1016/0003-9861(64)90482-5

Abstract

Active preparations of tryptophan synthetase were obtained from Bengal gram (Cicer arietinum) by the following procedure: (1) precipitation of inactive materials by manganous sulfate, (2) Adsorption of impurities on Alumina Cγ , (3) Adsorption of tryptophan synthetase on tricalcium phosphate gel, removal of inert protein from the gel by treatment with phosphate buffer (pH 7.2), and selective elution of the enzyme by 0.15 M phosphate buffer pH 7.2 containing 10% ammonium sulfate and 10-3M serine. A 220-fold purification of the enzyme with 44% recovery of the activity was achieved. The pH optimum, effect of temperature, and substrate concentration and other properties of the purified enzyme have been studied in detail. Only the l-isomer of serine takes part in the reaction. The Km values for indole, l-serine, and dl-serine were calculated to be 0.66, 4.1, and 8.6 × 10-4M, respectively. A kinetic study of the inhibition of tryptophan synthetase by indole-propionic acid has shown that it is of a competitive type. It has been demonstrated for the first time that 4-nitro-salicylaldehyde can replace pyridoxal phosphate as a coenzyme for the tryptophan synthetase reaction.

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ID Code:82612
Deposited On:14 Feb 2012 11:09
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