Results 151 to 160 of about 48,177 (188)

IMMUNOREACTIVE UROPORPHYRINOGEN DECARBOXYLASE IN PORPHYRIA CUTANEA TARDA

The Lancet, 1983
Immunoreactive uroporphyrinogen decarboxylase was measured by rocket immuno-electrophoresis in haemolysates from 7 unrelated patients with familial porphyria cutanea tarda (PCT), 6 patients with sporadic PCT, and 7 normal subjects. In all patients with familial PCT immunoreactive enzyme protein was decreased (51% of normal), to the same extent as ...
G H, Elder, D M, Sheppard, J A, Tovey, A J, Urquhart   +3 more
openaire   +2 more sources

Genetics and pathogenesis of human uroporphyrinogen decarboxylase defects

Clinical Biochemistry, 1989
Two types of human porphyria, porphyria cutanea tarda (PCT) and hepatoerythropoietic porphyria (HEP), result from partial deficiency of uroporphyrinogen decarboxylase (UROD). About 20% of patients with PCT have a 50% decrease in UROD concentration in all tissues that is inherited as an autosomal dominant trait with low penetrance (type II PCT).
G H, Elder, A G, Roberts, R E, de Salamanca   +2 more
openaire   +2 more sources

Uroporphyrinogen Decarboxylase Deficiency in Experimental Chronic Hepatic Porphyria

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1980
During hexachlorobenzene feeding of rats the following biochemical signs of a chronic hepatic porphyria developed: porphyrinuria with increase of uro- and hexacarboxyporphyrin, hepatic prophyrin accumulation of uro- and heptacarboxyporphyrin and a diminished activity of uroporphyrinogen decarboxylase in the liver, but nut in the red cells. During the 5.
R, von Tiepermann, G, Koss, M, Doss
openaire   +2 more sources

Decreased uroporphyrinogen decarboxylase activity in ‘experimental symptomatic porphyria’

Life Sciences, 1971
Abstract An experimental porphyria resembling human acquired symptomatic porphyria from the biochemical viewpoint was induced in rats by prior iron overload followed by the feeding of hexachlorobenzene (HCB). The characteristic accumulation of 8- and 7-carboxyl porphyrins in the livers of these animals suggested a possible defect of decarboxylation ...
J J, Taljaard, B C, Shanley, S M, Joubert   +2 more
openaire   +2 more sources

Measurement of the uroporphyrinogen decarboxylase activity in blood

Scandinavian Journal of Clinical and Laboratory Investigation, 1982
A method for measuring uroporphyrinogen decarboxylase activity is described. The method measures uroporphyrinogen decarboxylase activity equally sensitively using either uroporphyrinogen I or III as substrate.Using this method uroporphyrinogen decarboxylase activity was measured in the erythrocytes and enriched reticulocytes of healthy normal persons ...
M, Salmi, R, Tenhunen
openaire   +2 more sources

Cell-free translation of human uroporphyrinogen decarboxylase mRNAs

Biochemical and Biophysical Research Communications, 1984
Uroporphyrinogen decarboxylase was synthesized in a reticulocyte lysate cell-free system under the direction of messenger RNAs isolated from human fetal liver and from human reticulocytes. The enzyme was specifically isolated by immuno affinity chromatography.
B, Grandchamp, P H, Roméo, H, de Verneuil, A, Dubart, M, Goossens, J, Rosa, Y, Nordmann   +6 more
openaire   +2 more sources

Metal Alteration of Uroporphyrinogen Decarboxylase and Coproporphyrinogen Oxidasea

Annals of the New York Academy of Sciences, 1987
Both UD and CO are susceptible to alteration by sulfhydryl-directed binding agents including a variety of trace metals. UD apparently requires a functional SH group or groups for catalytic activity, and the various steps of decarboxylation catalyzed by the enzyme can be differentially inhibited by divalent cations such as Hg2+ at very low ...
J S, Woods, B A, Fowler
openaire   +2 more sources

Mouse uroporphyrinogen decarboxylase: CDNA cloning, expression, and mapping

Mammalian Genome, 1996
Uroporphyrinogen decarboxylase (URO-decarboxylase; EC 4.1.1.37), the heme biosynthetic enzyme responsible for the conversion of uroporphyrinogen III to coproporphyrinogen III, is the enzymatic defect in porphyria cutanea tarda, the most common porphyria. The mouse URO-decarboxylase cDNA was isolated from a mouse adult liver cDNA library.
C, Wu, W, Xu, C A, Kozak, R J, Desnick
openaire   +2 more sources

AML-144 Uroporphyrinogen Decarboxylase (UROD) Is a Therapeutically Targetable Dependency in Acute Erythroid Leukemia.

Clinical Lymphoma, Myeloma & Leukemia, 2022
Jake Friske, Y. Fukuda, Emily A Backhaus, Pradyuamna Baviskar, Francesca Benini, J. Connelly, Jonathon D. Klein, T. Cunningham, Jiyang Yu, S. Pruett-Miller, J. Schuetz, C. Mullighan, Ilaira lacobucci   +12 more
semanticscholar   +1 more source

Cloning of Chlorobium Uroporphyrinogen Decarboxylase Gene

1998
Chlorobium, the green sulfur bacterium, is one of the early forms of life that evolved a photosynthetic system and synthesizes large amounts of tetrapyrroles (1–3). The present-day Chlorobiaceae, often found in the gloomy depths of ponds and lakes where H2S and CO2 are in abundance but the light intensity is extremely low, have been shown to contain ...
Debabrata Majumdar, Kaiping Xu, Victoria Ndivo   +2 more
openaire   +1 more source