Biosynthesis in vitro of tryptophanase by polyribosomes from induced cultures of Escherichia coli
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چکیده
منابع مشابه
Polyribosomes of Escherichia coli
Growing cells incubated in a medium lacking glucose undergo a rapid breakdown of polyribosomes to single ‘70 S ribosomes. This conversion is accompanied by a loss of protein-synthetic capacity in vivo and is inhibited by chloramphenicol, but not by puromycin. The conversion of polysomes to 70 S ribosomes, with a half-life of 1: to 24 min at 37’, appears to reflect a breakdown of messenger ribon...
متن کاملPolyribosomes of Escherichia coli
Growing cells incubated in a medium lacking glucose undergo a rapid breakdown of polyribosomes to single ‘70 S ribosomes. This conversion is accompanied by a loss of protein-synthetic capacity in vivo and is inhibited by chloramphenicol, but not by puromycin. The conversion of polysomes to 70 S ribosomes, with a half-life of 1: to 24 min at 37’, appears to reflect a breakdown of messenger ribon...
متن کاملRepression of Tryptophanase Synthesis in Escherichia Coli.
Beggs, William H. (University of Cincinnati, Cincinnati, Ohio), and Herman C. Lichstein. Repression of tryptophanase synthesis in Escherichia coli. J. Bacteriol. 89:996-1004. 1965.-The nature of the glucose effect on tryptophanase in Escherichia coli (Crookes) was investigated to test the catabolite-repression hypothesis. Under static conditions of growth in the presence of 0.005 m glucose, try...
متن کاملEscherichia coli tryptophanase in the enteric environment.
The activity of the enzyme tryptophanase in the enteric environment was investigated to elucidate the significance of the enzyme in the metabolism of Escherichia coli. The tryptophanase activity, tryptophan content, and indole concentration as well as the numbers of E. coli were determined in the intestinal and fecal contents of conventional, germ-free, and monocontaminated axenic laboratory mi...
متن کاملEssential 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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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1971
ISSN: 0306-3283
DOI: 10.1042/bj1230355