Results 161 to 170 of about 4,609 (210)
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The enzymatic inactivation of porphobilinogen deaminase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract 1. 1. Porphobilinogen deaminase was inhibited by pyrrolooxygenase, a mixed-function oxidase which inhibits tryptophan-containing enzymes in the presence of sodium dithionite. 2. 2. Both enzymes were isolated from wheat germ but it was found that pyrrolooxygenase acted on deaminases from different origins. 3. 3.
R B, Frydman, B, Frydman
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Interaction of analogues of porphobilinogen with porphobilinogen deaminase

Journal of the Chemical Society, Perkin Transactions 1, 1996
2-Methylporphobilinogen 5 and 8,9-didehydroporphobilinogen 7 are only weak inhibitors of porphobilinogen deaminase (hydroxymethylbilane synthase). The phosphonate analogue 8 and 9-fluoroporphobilinogen 9 are good inhibitors, however, and also act as slow substrates (the first unnatural substrates known for this enzyme).
Finian J. Leeper, Martin Rock
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Characterization of porphobilinogen deaminase from rat liver

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
Porphobilinogen deaminase (porphobilinogen ammonia-lyase, EC 4.3.1.8) was isolated from rat liver. The final preparation was homogeneous according to polyacrylamide gel electrophoresis and immunodiffusion criteria. Electrophoresis of the native enzyme revealed a single band of activity which was distributed into three bands after incubation with ...
M B, Mazzetti, J M, Tomio
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Porphobilinogen deaminase gene structure and molecular defects

Journal of Bioenergetics and Biomembranes, 1995
Porphobilinogen deaminase (PBGD) is the third enzyme of the heme biosynthetic pathway. The half-normal activity of human PBGD causes acute intermittent porphyria (AIP), an autosomal dominant inherited disease. Two PBGD isoforms, one ubiquitous and one erythroid specific, are encoded by a single gene localized to chromosomal region 11q24.1-11q24.2.
J C, Deybach, H, Puy
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Systematic specificity studies on porphobilinogen deaminase

Bioorganic & Medicinal Chemistry Letters, 1994
Abstract Analogs of porphobilinogen (PBG) with different arrangements of the acidic side chains at C-3 and C-4 were tested for their ability to form complexes (ESx, x = 1–4) with PBG deaminase (EC 4.3.1.8), the enzyme responsible for the tetramerization of PBG into hydroxymethylbilane (HMB).
Karen R. Clemens   +5 more
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Protoporphyrinogen oxidase and porphobilinogen deaminase in variegate porphyria

European Journal of Clinical Investigation, 1986
Abstract. Two enzymes of the haem biosynthetic pathway were investigated in patients with variegate porphyria. Protoporphyrinogen oxidase in cultures of Epstein‐Barr virus transformed lymphoblasts from twenty‐seven patients showed a mean maximal velocity (Vmax) of 0·39 ± 0·08+ nmol of protoporphyrin mg protein‐1 h‐1, a 52% reduction (P < 0·001 ...
P N, Meissner   +4 more
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ELISA for measuring porphobilinogen deaminase in human erythrocytes

Clinica Chimica Acta, 1989
An ELISA method has been developed to quantitate human porphobilinogen deaminase in erythrocyte lysate. The antiserum used in the assay was raised against the erythropoietic form of human porphobilinogen deaminase. The IgG fraction was characterized by use of immunoblotting technique, rocket immunoelectrophoresis and immunotitration and shown to be ...
L, Lannfelt   +4 more
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Erythrocyte porphobilinogen deaminase activity and primary liver cancer

Journal of Internal Medicine, 1995
Abstract. Objectives. To study whether primary liver cancer (PLC) could be associated with acute intermittent porphyria (AIP) carriership and whether the activity of erythrocyte porphobilinogen deaminase (PBGD) could be used as a tumour marker for PLC.Design. Prospective study.Setting.
J, Kaczynski   +4 more
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