Determination of Amine Oxidases

Kapeller‐Adler, R.

doi:10.1002/9780470110409.ch2

Cited by 22 publications

(19 citation statements)

References 93 publications

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“…Even though this assay was criticized by Green et al [24] on the basis that the benzaldehyde formed is further metabolized by aldehyde dehydrogenase present in liver mitochondria, the validity for the application of this method has been established by Schnaitman and Greenawalt [25]. The absorption coefficient of 12mM-' cm-' for benzaldehyde at 250nm was used in calculating the enzyme activity [26].…”

Section: Enzyme Assuysmentioning

confidence: 99%

NADH‐Dependent Aryl Hydrocarbon Hydroxylase in Rat Liver Mitochondrial Outer Membrane

Uemura

Chiesara

1976

European Journal of Biochemistry

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NADH‐dependent 3,4‐benzpyrene hydroxylase activity was detected in the purified mitochondrial outer membrane fraction from the livers of rats treated with 3‐methylcholanthrene. The specific activity in the outer membrane fraction is nearly equal to that of microsomes, a level too high to be accounted for only by the microsomal contamination. On the other hand, the NADPH‐dependent 3,4‐benzpyrene hydroxylase activity in the outer membrane fraction is about 50% of that of microsomes. The ratio of the specific activity of NADPH‐ to NADH‐dependent 3,4‐benzpyrene hydroxylase in microsomal fraction was about 3.5, while that of the outer membrane fraction was about 1.5. Moreover, it was found that NADH‐dependent 3,4‐benzpyrene hydroxylase activity in mitochondrial outer membrane from control rat liver was cyanide‐insensitive, while that in microsomes was cyanide‐sensitive. These results suggest the presence in the mitochondrial outer membrane fraction of aryl hydrocarbon hydroxylase activity which uses as electron donor NADH nearly to the same extent as NADPH. The hydroxylase system is composed of cyanide‐insensitive cytochrome P‐450 and is inducible markedly by 3‐methylcholanthrene treatment. The probable electron transfer pathways in the mitochondrial outer membrane cytochrome P‐450 oxidase system are discussed.

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Section: Enzyme Assuysmentioning

confidence: 99%

NADH‐Dependent Aryl Hydrocarbon Hydroxylase in Rat Liver Mitochondrial Outer Membrane

Uemura

Chiesara

1976

European Journal of Biochemistry

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“…This reaction was completely inhibited by the specific MAO inhibitors iproniazid, pargyline or tranylcypromide (0.1 mM), but not by isoniazid (I .O mM), phenylhydrazine or aminoguanidine (0.1 mM), which inhibit DA0 activity [4].…”

Section: Liberation Of Nh3 (Ormentioning

confidence: 99%

“…The activity of DA0 is inhibited by carbonyl reagents but not by MAO inhibitors [8]. No flavin components or free SH groups were found in preparations of DA0 [4]. An important criterion for distinction between MAO and DA0 is the fact, established by Blaschko [ 9, lo] , that only MAO possess the ability to attack secondary amines (for example, N-methyl&phenylethylamine) with liberation of methylamine.…”

Section: Introductionmentioning

confidence: 99%

“…MAO catalyze the oxidative deamination of biogenic monoamines; this reaction is inhibited by specific MAO inhibitors (pargyline, tranylcypromine) but not by carbonyl reagents. DA0 belongs to the category of pyridoxal phosphate dependent enzymes [4]. The activity of DA0 is inhibited by carbonyl reagents but not by MAO inhibitors [8].…”

Section: Introductionmentioning

confidence: 99%

“…There are two main groups of amine oxidases [4] : monoamine oxidases (MAO) (EC 1.4.3.4) and diamine oxidases (DAO) (EC 1. 4.3.6).…”

Section: Introductionmentioning

confidence: 99%

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