Direct Kinetic Evidence for Triplet State Energy Transfer from Escherichia coli Alkaline Phosphatase Tryptophan 109 to Bound Terbium
نویسندگان
چکیده
منابع مشابه
Escherichia coli alkaline phosphatase. Kinetic studies with the tetrameric enzyme.
1. The stability of the tetrameric form of Escherichia coli alkaline phosphatase was examined by analytical ultracentrifugation. 2. The stopped-flow technique was used to study the hydrolysis of nitrophenyl phosphates by the alkaline phosphatase tetramer at pH7.5 and 8.3. In both cases transient product formation was observed before the steady state was attained. Both transients consisted of th...
متن کاملLethality of Streptomycin for Alkaline Phosphatase Constitutive Escherichia Coli.
Rosenkranz, Herbert S. (Columbia University, New York, N.Y.) and Howard S. Carr. Lethality of streptomycin for alkaline phosphatase constitutive Escherichia coli. J. Bacteriol. 85:751-753. 1963.-An alkaline phosphatase constitutive strain of Escherichia coli was more sensitive to streptomycin in a phosphorus-rich medium than was the wild parent strain. In a low-phosphorus medium, the efficiency...
متن کاملFunctional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase.
Escherichia coli alkaline phosphatase (AP) is a proficient phosphomonoesterase with two Zn(2+) ions in its active site. Sequence homology suggests a distant evolutionary relationship between AP and alkaline phosphodiesterase/nucleotide pyrophosphatase, with conservation of the catalytic metal ions. Furthermore, many other phosphodiesterases, although not evolutionarily related, have a similar a...
متن کاملSecretion of alkaline phosphatase subunits by spheroplasts of Escherichia coli.
Under conditions that permitted continued protein synthesis, spheroplasts of Escherichia coli were unable to form active alkaline phosphatase, although they synthesized protein that was antigenically related to alkaline phosphatase subunits. This cross-reacting protein was primarily detected in the medium of the spheroplast culture, and it had properties that closely resembled those of the alka...
متن کاملOsmoregulation of alkaline phosphatase synthesis in Escherichia coli K-12.
Alkaline phosphatase, the phoA product, is synthesized constitutively in phoR mutants. This constitutive synthesis, which is independent of phosphate control, varies with changes in the osmolarity of the growth medium; phoA expression increases with increasing osmolarity. Maximum expression of the osmoregulated genes phoA, ompC, and ompF was achieved by osmotic manipulation of minimal medium; c...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.39.22890