Essential arginine residues in tryptophanase from Escherichia coli.
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منابع مشابه
Essential arginine residues in tryptophanase from Escherichia coli.
Tryptophanase from Escherichia coli B/1t7-A is inactivated by the arginine-specific reagent, phenylglyoxal, in potassium phosphate buffer at pH 7.8 AND 25 degrees. Apo- and holoenzyme are inactivated at the same rate, and inactivation of both is correlated with modification of 2 arginine residues/tryptophanase monomer. Substrate analogs having a carboxyl group protect the holoenzyme against bot...
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Biosynthetic arginine decarboxylase of Escherichia coli has been purified 1,500-fold. The purified enzyme showed two bands on disc gel electrophoresis, both carrying out the decarboxylation of L-arginine. Electrophoresis in the presence of sodium dodecyl sulfate and sedimentation equilibrium ultracentrifugation was consistent with the enzyme being a tetramer of approximately 296,000 molecular w...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)41008-8