Spectrophotometric assay for measuring mannitol oxidase activity v1 (protocols.io.naudaew)

protocols.io ◽  
2018 ◽  
Author(s):  
Alexandre Lobo ◽  
V tor
Keyword(s):  
Oxidase Activity ◽  
Spectrophotometric Assay

A spectrophotometric assay for monoamine oxidase activity with 2, 4-dinitrophenylhydrazine as a derivatized reagent

2016 ◽  
Vol 512 ◽  
pp. 18-25 ◽  
Author(s):  
Guili Huang ◽  
Fei Zhu ◽  
Yuhang Chen ◽  
Shiqiang Chen ◽  
Zhonghong Liu ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Oxidase Activity ◽  
Spectrophotometric Assay ◽  
Monoamine Oxidase Activity

scholarly journals A kinetic investigation of the acyl-CoA oxidase reaction with the use of a novel spectrophotometric assay. Inhibition by acetyl-CoA, CoA and FMN

1989 ◽  
Vol 263 (1) ◽  
pp. 297-299 ◽  
Author(s):  
R Hovik ◽  
H Osmundsen
Keyword(s):  
Oxidase Activity ◽  
Spectrophotometric Assay ◽  
Strong Absorption ◽  
Kinetic Investigation ◽  
Kinetic Characteristics ◽  
Direct Reading ◽  
Acetyl Coa ◽  
Acyl Coa Oxidase ◽  
Oxidase Reaction

A direct-reading spectrophotometric assay for acyl-CoA oxidase activity is described. The assay is based on the strong absorption at 300 nm of deca-2-trans,4-cis-dienoyl-CoA, the product of oxidation of dec-4-cis-enoyl-CoA. By use of this assay, acetyl-CoA, CoA and FMN were found to be inhibitors of acyl-CoA oxidase, but with distinctly different kinetic characteristics.

A rapid spectrophotometric assay of phenylpyruvate oxidase activity

1972 ◽  
Vol 50 (1) ◽  
pp. 180-186 ◽  
Author(s):  
Brian L. Goodwin ◽  
Elizabeth G. Werner
Keyword(s):  
Oxidase Activity ◽  
Spectrophotometric Assay

A New Continuous Spectrophotometric Assay Method for DOPA Oxidase Activity of Tyrosinase

2003 ◽  
Vol 22 (5) ◽  
pp. 473-480 ◽  
Author(s):  
Yong-Doo Park ◽  
Jae-Rin Lee ◽  
Kyung-Hee Park ◽  
Hwa-Sun Hahn ◽  
Myong-Joon Hahn ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Spectrophotometric Assay ◽  
Assay Method ◽  
Dopa Oxidase

scholarly journals A sensitive spectrophotometric assay for peroxisomal acyl-CoA oxidase

1985 ◽  
Vol 227 (1) ◽  
pp. 205-210 ◽  
Author(s):  
G M Small ◽  
K Burdett ◽  
M J Connock
Keyword(s):  
Oxidase Activity ◽  
Mouse Liver ◽  
Enzyme Concentration ◽  
Fatty Acyl ◽  
Spectrophotometric Assay ◽  
Acid Oxidase ◽  
Rat Intestine ◽  
Amino Acid Oxidase ◽  
Acyl Coa Oxidase ◽  
First Time

A simple spectrophotometric assay was developed for peroxisomal fatty acyl-CoA oxidase activity. The assay, based on the H2O2-dependent oxidation of leuco-dichlorofluorescein catalysed by exogenous peroxidase, is more sensitive than methods previously described. By using mouse liver samples, cofactor requirements were assessed and a linear relationship was demonstrated between dye oxidation and enzyme concentration. By using this assay on subcellular fractions, palmitoyl-CoA oxidase activity was localized for the first time in microperoxisomes of rat intestine. The assay was also adapted to measure D-amino acid oxidase activity, demonstrating the versatility of this method for measuring activity of other H2O2-producing oxidases.

New Spectrophotometric Assay for Polyphenol Oxidase Activity

1993 ◽  
Vol 215 (1) ◽  
pp. 59-65 ◽  
Author(s):  
F. Gauillard ◽  
F. Richardforget ◽  
J. Nicolas
Keyword(s):  
Polyphenol Oxidase ◽  
Oxidase Activity ◽  
Spectrophotometric Assay ◽  
Polyphenol Oxidase Activity

Mitochondrial Oxidation of p-N, N-Dimethylamino-β-Phenethylamine (DAPA)

1975 ◽  
Vol 33 ◽  
pp. 458-459
Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman
Keyword(s):  
Guinea Pig ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Histochemical Demonstration ◽  
Guinea Pig Heart ◽  
Pig Kidney ◽  
Cytoplasmic Vacuoles ◽  
Liver And Kidney ◽  
Mitochondrial Oxidation ◽  
Amine Oxidase Activity

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.

Sign in / Sign up

Export Citation Format

Share Document