منابع مشابه
Stereospecificity of hepatic L-tryptophan 2,3-dioxygenase.
Tryptophan 2,3-dioxygenase [L-tryptophan--oxygen 2,3-oxidoreductase (decyclizing), EC 1.13.11.11] has been reported to act solely on the L-isomer of tryptophan. However, by using a sensitive assay method with D- and L-[ring-2-14C]tryptophan and improved assay conditions, we were able to demonstrate that both the D- and L-stereoisomers of tryptophan were cleaved by the supernatant fraction (3000...
متن کاملHepatic and lipoprotein lipases selectively assayed in postheparin plasma.
Sensitive, reliable procedures are reported for the selective assay of lipoprotein lipase (LPL) and hepatic lipase (HL) in postheparin plasma samples. LPL is inhibited in the HL assay by inclusion of 0.76 mol/L sodium chloride in the substrate. In the LPL assay, specificity is attained by pretreating the sample with sodium dodecyl sulfate, which selectively denatures HL. This LPL method was val...
متن کاملStereospecificity of aminoglycoside-ribosomal interactions.
Aminoglycoside antibiotics bind to the A-site decoding region of bacterial rRNA causing mistranslation and/or premature message termination. Aminoglycoside binding to A-site RNA decoding region constructs is established here to be only weakly stereospecific. Mirror-image prokaryotic A-site decoding region constructs were prepared in the natural D-series and the enantiomeric L-series and tested ...
متن کاملStereospecificity of Monoamine Oxidase Inhibitors
Pretreatment with two doses of reserpine (each 0.1 mg/kg, intraperitoneally) sensitizes the heart to the positive chronotropic action of norepinephrine and reduces the response to stimulation of the accelerans nerve. Ganglionic transmission remains unaffected. The results indicate that the presence of certain stores of peripheral sympathetic transmitter is essential for the production of tachyc...
متن کاملInversion of stereospecificity of vanillyl-alcohol oxidase.
Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these reactions is the stereospecific hydroxylation of 4-ethylphenol-forming (R)-1-(4'-hydroxyphenyl)ethanol. D...
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: FEBS Letters
سال: 1976
ISSN: 0014-5793
DOI: 10.1016/0014-5793(76)80941-6