Results 111 to 120 of about 2,459 (167)

Protoporphyrinogen oxidase and ferrochelatase in porphyria variegata

European Journal of Clinical Investigation, 1983
Abstract. Protoporphyrinogen oxidase activity and ferrochelatase activity were measured in leucocytes from patients with porphyria variegata. The mean activity of protoporphyrinogen oxidase (PPO) in porphyria variegata (PV) was about 50% of normal (P < 0.05). The mean activity of ferrochelatase with 59Fe2+ sulphate and protoporphyrin as substrates (
D J, Viljoen, R, Cummins, J, Alexopoulos, S, Kramer   +3 more
exaly   +3 more sources

Mitochondrial targeting of human protoporphyrinogen oxidase

Cell Biology International, 2006
Variegate porphyria is an autosomal dominant disorder of heme metabolism resulting from a deficiency in protoporphyrinogen oxidase, an enzyme located on the inner mitochondrial membrane. This study examined the effect of three South African VP-causing mutations (H20P, R59W, R168C) on mitochondrial targeting.
Lester M, Davids, Anne V, Corrigall, Peter N, Meissner   +2 more
exaly   +3 more sources

Tetrahydrophthalimidobenzoates as protoporphyrinogen IX oxidase inhibiting herbicides

Pesticide Biochemistry and Physiology, 2017
Tetrahydrophthalimidobenzoates are a class of protoporphyrinogen oxidase herbicides acting on the protoporphyrinogen oxidase enzyme. After the discovery of compound 1, a series of novel tetrahydrophthalimidobenzoate derivatives were designed and synthesized, and some synthesized compounds exhibited good herbicidal activity in controlling broadleaf ...
Lin Chen
exaly   +3 more sources

The mitochondrial location of protoporphyrinogen oxidase

European Journal of Biochemistry, 1985
Using the digitonin method and subsequent fractionation of rat liver mitochondria, protoporphyrinogen oxidase (penultimate enzyme in the heme biosynthesis pathway) was found to be closely associated with the mitochondrial inner membrane fraction.Chemical treatment with non‐specific probes (trypsin and diazobenzene sulfonate) of either intact or ...
J C, Deybach, V, da Silva, B, Grandchamp, Y, Nordmann   +3 more
openaire   +2 more sources

RRM analysis of protoporphyrinogen oxidase

Australasian Physics & Engineering Sciences in Medicine, 2004
Enzymes are crucial in accelerating metabolic reactions in living organisms. Protoporphyrinogen oxidase (PpOI) is an enzyme that catalyses the production of protoporphyrin IX (PpIX), a protein used in a cancer treatment known as photodynamic therapy (PDT).
M, Sauren, E, Pirogova, I, Cosic
openaire   +2 more sources

Measurement of Protoporphyrinogen Oxidase Activity

Current Protocols in Toxicology, 1999
AbstractProtoporphyrinogen oxidase catalyzes the oxidation of protoporphyrinogen to protophyrin. It is a membrane‐bound mitochondrial enzyme and it is the target of photobleaching herbicides. The basic assay presented in this unit for measuring oxidase activity is based on oxidation of the colorless, nonfluorescent substrate, protoporphyrinogen, to the
J M, Jacobs, N J, Jacobs
openaire   +2 more sources

Fluorometric assays for coproporphyrinogen oxidase and protoporphyrinogen oxidase

Analytical Biochemistry, 1985
We describe fluorometric assays for two enzymes of the heme pathway, coproporphyrinogen oxidase and protoporphyrinogen oxidase. Both assays are based on measurement of protoporphyrin IX fluorescence generated from coproporphyrinogen III by the two consecutive reactions catalyzed by coproporphyrinogen oxidase and protoporphyrinogen oxidase.
P, Labbe, J M, Camadro, H, Chambon
openaire   +2 more sources

Characteristics of Protoporphyrinogen Oxidase

1999
Protoporphyrinogen oxidase (EC 1.3.3.4) catalyzes the oxidative O2-dependent aromatization of the colorless protoporphyrinogen IX to the highly conjugated protoporphyrin IX, the precursor of both hemes and chlorophylls (Fig. 1). It is the final enzyme in the common branch of the heme and chlorophyll biosyn-thetic pathways in plants (Fig. 2).
Camadro, J.M., Arnould, S., Le Guen, L., Santos, Raphael, Matringe, Michel, Mornet, R.   +5 more
openaire   +2 more sources

Purification and characterization of murine protoporphyrinogen oxidase

Biochemistry, 1987
The penultimate enzyme of the heme biosynthetic pathway, protoporphyrinogen oxidase (EC 1.3.3.4), has been purified to apparent homogeneity from mouse liver mitochondria. The purification involves solubilization from mitochondrial membranes with sodium cholate followed by ammonium sulfate fractionation and gel filtration on a Sepharose CL-6B column ...
H A, Dailey, S W, Karr
openaire   +2 more sources