منابع مشابه
Improved enzymatic assay of chloramphenicol.
We partly purified R-factor-encoded chloramphenicol acetyltransferase (EC 2.3.1.28) from a highly choloramphenicol-resistant mutant derived from Escherichia coli W677/R5. The preparation permitted rapid quanitation of chloramphenicol by use of [14C]acetylcoenzyme A, removing the diacetylated product by selective adsorption onto micropore filters. Succinyl and glucuronyl 3-hydroxyl esters of chl...
متن کاملEnzymatic assay for spermidine.
The polyamine spermidine (NH,(CH&NH(CH&NH,) is widespread in nature. It is present in mammalian tissues (1, 2), plants (3), bacteria (47), ribosomes (6, 8), and bacteriophages (9-11). There are various methods for its identification, including steam distillation (12)) paper chromatography (13-18)) paper electrophoresis (14, 16, 17, 19), ion exchange chromatography (2, 5), gas chromatography (31...
متن کاملImproved methods for the solubilization and assay of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase.
A method for solubilizing HMG-CoA reductase is described that reproducibly yielded approximately 190% of the activity assayed in rat liver microsomes. Optimal solubilization occurred when microsomal membranes were frozen at a fixed concentration, thawed, homogenized in a buffer containing 50% glycerol, and incubated at 37 degrees C for 60 minutes. A rapid spectrophotometric assay of the reducta...
متن کاملImproved methods for the assay and activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase.
A simple and rapid mixed-phase method for the quantitative assay of 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase and a procedure for the efficient reactivation of Mg-ATP-inactivated microsomal HMG-CoA reductase by potato acid phosphatase are described. The mixed-phase assay entails the direct addition of the acidified, deproteinized incubation mixture to a toluene-based scintillation fluor. T...
متن کاملThe Enzymatic Carboxylation of Propionyl Coenzyme A
(R)and (S)-Z-deuteriopropionyl coenzyme A of approximately 75% optical purity were prepared by a series of reactions starting from optically pure alanine. With these compounds as substrates for propionyl-CoA carboxylase, the deuterium isotope effect was found to be small and probably secondary. No tritium isotope effect was observed when enzymatically prepared 2-3H-propionyl-CoA was used as sub...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1951
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)56124-x