Results 141 to 150 of about 48,177 (188)

Decreased hepatic uroporphyrinogen decarboxylase activity in porphyria cutanea tarda.

New England Journal of Medicine, 1982
To test whether reduced hepatic uroporphyrinogen decarboxylase activity is a specific and intrinsic defect in porphyria cutanea tarda, we measured enzymatic activity in the livers of 17 patients with porphyria cutanea tarda, 12 "normal" control patients without liver disease, and 41 patients with other forms of porphyria, alcoholic liver disease ...
B. Felsher, N. Carpio, D. W. Engleking, A. Nunn   +3 more
semanticscholar   +3 more sources

Uroporphyrinogen decarboxylase: optimizing radiotherapy for head and neck cancer.

Future Oncology, 2011
Emma Ito, K. Yip, Fei-Fei Liu
semanticscholar   +3 more sources

Uroporphyrinogen decarboxylase

Journal of Bioenergetics and Biomembranes, 1995
Uroporphyrinogen decarboxylase (EC 4.1.1.37) catalyzes the decarboxylation of uroporphyrinogen III to coproporphyrinogen III. The amino acid sequences, kinetic properties, and physicochemical characteristics of enzymes from different sources (mammals, yeast, bacteria) are similar, but little is known about the structure/function relationships of ...
G H, Elder, A G, Roberts
openaire   +2 more sources

Hepatoerythropoietic Porphyria Caused by a Novel Homoallelic Mutation in Uroporphyrinogen Decarboxylase Gene in Egyptian Patients.

Folia biologica, 2015
Porphyrias are metabolic disorders resulting from mutations in haem biosynthetic pathway genes. Hepatoerythropoietic porphyria (HEP) is a rare type of porphyria caused by the deficiency of the fifth enzyme (uroporphyrinogen decarboxylase, UROD) in this ...
Farrag Ms, Ivan Mikula, E. Richard, Saudek, H. DeVerneuil, Pavel Martásek   +5 more
semanticscholar   +1 more source

Measurement of Uroporphyrinogen Decarboxylase Activity

Current Protocols in Toxicology, 1999
AbstractUroporphyrinogen decarboxylase (UROD) catalyzes decarboxylation of the four acetate side chains of urophyrinogen to form coproporphyrinogen. Activity of UROD can be measured using an enzymatically prepared substrate or a chemically prepared one.
J D, Phillips, J P, Kushner
openaire   +2 more sources

Uroporphyrinogen decarboxylase from mouse spleen

Biochimica et Biophysica Acta (BBA) - General Subjects, 1971
Abstract An activity purified 21-fold from hematopoietic mouse spleen catalyzes the decarboxylaton of uroporphyrinogens I and III to stoichiometrically equivalent amounts of the corresponding coproporphyrinogens. Kinetic and stability studies indicate that the same enzyme system is involved in the two reactions.
G, Romeo, E Y, Levin
openaire   +2 more sources

Mutational analysis of human uroporphyrinogen decarboxylase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
Uroporphyrinogen decarboxylase (URO-D), a heme biosynthetic enzyme, catalyzes the multi-step decarboxylation reaction converting uroporphyrinogen I or III to coproporphyrinogen I or III. The URO-D protein has been purified from several sources and its gene has been cloned from many organisms.
E E, Wyckoff, J D, Phillips, A M, Sowa, M R, Franklin, J P, Kushner   +4 more
openaire   +2 more sources

Random decarboxylation of uroporphyrinogen III by human hepatic uroporphyrinogen decarboxylase

Journal of Chromatography B: Biomedical Sciences and Applications, 1991
The type III heptacarboxylic porphyrinogens derived from enzymic decarboxylation of an acetic acid substituent on uroporphyrinogen III to a methyl group by human hepatic uroporphyrinogen decarboxylase has been analysed by reversed-phase high-performance liquid chromatography with electrochemical detection.
J L, Luo, C K, Lim
openaire   +2 more sources