Alcohol dehydrogenase-coupled spectrophotometric assay of plasmalogenase

Freeman, Neil M.; Carey, Eric M.

doi:10.1016/0003-2697(83)90389-5

Cited by 9 publications

(1 citation statement)

References 22 publications

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“…Further, the amount of alcohol dehydrogenase in the reaction mixture (1 ml) is 38.5 jug of protein, which is a sufficient excess to reduce the aldehyde produced in the coupled-enzyme assay and the [S].s < Km for S can be maintained throughout the incubation period. The spectrofluorimetric assay is more sensitive than the spectrophotometric assay procedures described by previous investigators (Freeman & Carey, 1983;Arthur et al, 1986;Hirashima et al, 1989;Jurkowitz-Alexander et al, 1989). Fluorescence changes in control cuvettes are very small and stable compared with absorbance changes monitored spectrophotometrically at 340 nm.…”

Section: Discussionmentioning

confidence: 93%

Fluorimetric coupled enzyme assay for lysoplasmalogenase activity in liver

Hirashima

Farooqui

Horrocks

1989

Biochemical Journal

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We developed a continuous spectrofluorimetric assay of lysoplasmalogenase activity with the use of horse liver alcohol dehydrogenase as a coupling enzyme. In this method the disappearance of NADH is measured spectrofluorimetrically. The excitation and emission monochromators were set at 340 and 460 nm respectively. The assay is 10 times as sensitive as the previous u.v. spectrophotometric method. We could detect approx. 0.02 nmol of aldehyde produced/min per ml.

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Section: Discussionmentioning

confidence: 93%

Fluorimetric coupled enzyme assay for lysoplasmalogenase activity in liver

Hirashima

Farooqui

Horrocks

1989

Biochemical Journal

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Receptor-Mediated Degradation of Choline Plasmalogens and Glycerophospholipid Methylation: A New Hypothesis

Horrocks

Harder

Mozzi

et al. 1986

Enzymes of Lipid Metabolism II

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Biochemical changes in cuprizone-induced spongiform encephalopathy

Carey

Freeman

1983

Neurochem Res

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Cuprizone (biscyclohexanone oxaldihydrazone) which is known to produce a status spongiosus and demyelination in the CNS was administered in the diet of weanling male mice at a concentration of 0.4% by weight for a period of six weeks before returning animals to a normal diet. Changes in body weight but not brain weight were reversible. Based on the decline in CNP'ase activity and the concentration of galactocerebroside, the loss of myelin was around 70% in those sections of the cerebrum with a high content of white matter while the cerebellum was less affected. The activity of oligodendroglial HFA-ceramide galactosyl transferase was also reduced. These biochemical parameters of myelination were increased after withdrawal of Cuprizone. Remyelination in the cerebrum but not the cerebellum was incomplete. The activity of plasmalogenase hydrolysing the alkenyl group of alkenyl, acyl-phospholipids increased 2-fold in those sections in which myelin loss was most severe. The increase preceded the greatest loss of myelin components (3 to 6 weeks on Cuprizone). The origin of the increased phospholipase activity in demyelinating tissue is discussed. Following myelination, there was a deficit in plasmalogenase activity particularly in the frontal cortex of the cerebrum, where the plasmalogen concentration was higher than in controls.

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Alcohol dehydrogenase-coupled spectrophotometric assay of plasmalogenase

Cited by 9 publications

References 22 publications

Fluorimetric coupled enzyme assay for lysoplasmalogenase activity in liver

Fluorimetric coupled enzyme assay for lysoplasmalogenase activity in liver

Receptor-Mediated Degradation of Choline Plasmalogens and Glycerophospholipid Methylation: A New Hypothesis

Biochemical changes in cuprizone-induced spongiform encephalopathy

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