Further Studies on Competition of Berberine with Pyridoxal Phosphate in the Tryptophanase System of Escherichia coli.
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چکیده
منابع مشابه
Kinetic and Equilibrium Studies on the Activation of Escherichia coli K12 Tryptophanase by Pyridoxal S-Phosphate and Monovalent Cations *
An improved purification of Escherichia coli K12 tryptophanase is presented. It is shown that the apoenzyme crystals, oxidized by exposure to air, can be reactivated by treatment with a reducing agent. The titration of sulfhydryl groups shows that four -SH groups are exposed end two are masked per protomer. The influence of two effecters, monovalent cations and the coenzyme pyridoxal S-phosphat...
متن کاملFunction of Pyridoxal Phosphate: Resolution and Purification of the Tryptophanase Enzyme of Escherichia Coli
Since Hopkins and Cole (1) demonstrated the formation of indole from tryptophan by Bacterium coli, numerous investigators have attempted to find the mechanism of this reaction (2-5). At least three mechanisms have been suggested. Woods (3) postulated an oxidat,ive degradation of tryptophan to yield indole, carbon dioside, water, and ammonia, 5 atoms of oxygen being used in the process. Baker an...
متن کاملKinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 5'-phosphate and monovalent cations.
An improved purification of Escherichia coli K12 tryptophanase is presented. It is shown that the apoenzyme crystals, oxidized by exposure to air, can be reactivated by treatment with a reducing agent. The titration of sulfhydryl groups shows that four --SH groups are exposed and two are masked per protomer. The influence of two effectors, monovalent cations and the coenzyme pyridoxal 5'-phosph...
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ژورنال
عنوان ژورنال: Chemical and Pharmaceutical Bulletin
سال: 1961
ISSN: 0009-2363,1347-5223
DOI: 10.1248/cpb.9.651