Immunological properties of protocatechuate 3, 4-dioxygenase isofunctional enzymes
نویسندگان
چکیده
منابع مشابه
Reaction mechanism of protocatechuate 3,4-dioxygenase.
We have observed that high SOD-like function (decomposition of superoxide anion) was observed for several iron(III) compounds with tripodal ligands and several oxovanadium(IV) compounds, and also that these compounds exhibit high catalytic activity for oxidative cleavage of 3,5-di-tert-butylcatechol in non-donating solvents such as dichloromethane or nitromethane. These are suggesting that the ...
متن کامل3 , 4 = Dioxygenase III
In the early stage of the reaction of protocatechuate 3,4dioxygenase, a new spectral species of the enzyme having a broad absorption band with a maximum between 500 and 520 nm was observed by using a stopped flow technique. The observed spectrum was distinct from those of the enzyme or the enzyme-protoacatechuic acid complex and its formation was absolutely dependent on the simultaneous presenc...
متن کاملOxygenated form of protocatechuate 3,4-dioxygenase, a non-heme iron-containing dioxygenase, as reaction intermediate.
A short-lived new spectral species of protocatechuate 3,4-dioxygenase, a trivalent non-heme iron-containing enzyme, was observed in the early stage of the reaction. This new spectral species was characterized by a broad absorption band with a maximum between 500 and 520 rnp, distinct from those of the enzyme or the enzyme-protocatechuic acid complex. It could be demonstrated only in the presenc...
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Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, is expressed by a variety of cells and tissues such as macrophages, dendritic cells, cells of the endocrine system and by the placenta. IFN- γ is the main inducer of this enzyme. IDO acts as an important defense mechanism of innate immunity against pathogens. It also has tumor suppressive activity and prolong...
متن کاملPurification and some properties of human 4-hydroxyphenylpyruvate dioxygenase (I).
4-Hydroxyphenylpyruvate dioxygenase (I-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating, decarboxylating), EC 1.13.11.27) has been purified 800-fold in 25% yield from human liver by a procedure involving ammonium sulfate fractionation of an acetone powder extract and chromatography on hydroxylapatite, sulfopropyl-Sephadex C-50, and triethylaminoethyl cellulose. The preparation obtaine...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1976
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.126.1.516-519.1976