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At least 775 records · Page 43Linked to original sources
PubMed1983

3-aminopyridine 1,N6-ethenoadenine dinucleotide phosphate: a fluorescent reagent for NADP-requiring enzymes.

3-Aminopyridine 1,N6-ethenoadenine dinucleotide phosphate (epsilon-AADP) was synthesized from 3-aminopyridine adenine dinucleotide phosphate by reaction with chloroacetaldehyde. The reaction was monitored by high-pressure liquid chromatography. The product, epsilon-AADP, was purified by ion-exchange chromatography followed by a Sephadex G-10 desalting process. Spectrophotometric and fluorimetric properties of epsilon-AADP were obtained at neutral pH. Diazotization of epsilon-AADP was documented by azodye formation at pH values below 3 and the diazotized derivative was shown to react rapidly with sulfhydryl compounds at neutrality. As an analog of NADP, epsilon-AADP was demonstrated to be an effective NADP-competitive inhibitor of NADP-requiring dehydrogenases, reductases, and an NAD glycohydrolase.

Adenine Nucleotides↗
PubMed1986

A fluorogenic, mixed-disulfide reagent for thiol assay.

The design and synthesis of the mixed disulfide (ortho-nitroaniline-N-ethyldithio) 2-[pyridyl-5-thioureido-N'-(5-fluorescein)] are described and the chemical and spectroscopic properties of this thiol-specific fluorogenic reagent are presented. The high reactivity and sensitivity of this reagent in thiol assay are demonstrated with low-molecular-weight thiols and with human carbonmonoxyhemoglobin and its subunits. Comparison with conventional absorption methods shows that at least 100 times less material is needed; moreover, high background absorbance or turbidity do not interfere with the assay.

Carboxyhemoglobin↗
PubMed1986

A new assay for N-hydroxyarylamine O-acetyltransferase: reduction of N-hydroxyarylamines through N-acetoxyarylamines.

A simple fluorometric assay for N-hydroxyarylamine O-acetyltransferase is described and compared with a nucleic acid-binding assay. The assay method is based on the finding that the highly mutagenic 2-hydroxyamino-6-methyldipyrido[1,2-a:3',2'-d]imidazole (N-OH-Glu-P-1) was reduced to the corresponding amine, 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole (Glu-P-1), through N-acetoxy-Glu-P-1 as the reactive intermediate in the presence of N-hydroxyarylamine O-acetyltransferase, acetyl-CoA, and a sulfhydryl compound. The formation of Glu-P-1 was determined by its characteristic fluorescence intensity at 445 nm with excitation wavelength at 376 nm. The reductive reaction was inhibited by the addition of tRNA, DNA, and poly(G), to which the enzymatic product, N-acetoxy Glu-P-1, bound effectively due to its electrophilic nature. Since the fluorometric assay for the O-acetyltransferase is rapid, simple, and sensitive as compared with the nucleic acid-binding method using radioisotope-labeled N-hydroxyarylamine, this method is applicable to the general assay for the formation of reactive N-acetoxy-Glu-P-1.

Acetyltransferases↗