ALA Dehydratase Porphyria

2012 ◽  
Keyword(s):  
Ala Dehydratase

Expression Levels of ALA Dehydratase as a Marker of ALA-PDT Efficacy

2010 ◽  
Author(s):  
Schauder Avital ◽  
Feuerstein Tamar ◽  
Malik Zvi ◽  
Leonardo Longo
Keyword(s):  
Expression Levels ◽  
Ala Dehydratase

ALA-dehydratase activity inZea mays L.

1985 ◽  
Vol 85 (3) ◽  
pp. 337-343 ◽  
Author(s):  
Luciano Scarponi ◽  
Piero Perucci ◽  
Mario Monotti
Keyword(s):  
Dehydratase Activity ◽  
Ala Dehydratase

Effect of Ethanol and Zinc on ALA-Dehydratase Activity in Red Blood Cells

Enzyme ◽  
1976 ◽  
Vol 21 (3) ◽  
pp. 248-252 ◽  
Author(s):  
M. Abdulla ◽  
Brigitta Haeger-Aronsen ◽  
S. Svensson
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Dehydratase Activity ◽  
Ala Dehydratase

Succinylacetone and δ-Aminolevulinic Acid Dehydratase in Hereditary Tyrosinemia: Immunochemical Study of the Enzyme

PEDIATRICS ◽  
1990 ◽  
Vol 86 (1) ◽  
pp. 84-86
Author(s):  
Shigeru Sassa ◽  
Hiroyoshi Fujita ◽  
Attallah Kappas
Keyword(s):  
Liver Transplantation ◽  
Metabolic Disorder ◽  
Aminolevulinic Acid ◽  
Potent Inhibitor ◽  
Enzyme Protein ◽  
Immunochemical Study ◽  
Acid Dehydratase ◽  
Hereditary Tyrosinemia ◽  
Ala Dehydratase

Immunochemical determinations of δ-aminolevulinic acid (ALA) dehydratase were performed in erythrocytes and in liver of a patient with hereditary tyrosinemia who underwent liver transplantation for correction of this metabolic disorder. Both erythrocytic and hepatic ALA dehydratase activities were extremely low before liver transplantation, but they appeared normal after transplantation. According to results of immunochemical quantification of ALA dehydratase, the level of the enzyme protein in erythrocytes was not different before, during, and after liver transplantation. Immunoguantifiable enzyme concentrations were not substantially different in the patient's own liver as compared with the transplanted liver. These findings indicate that although succinylacetone, an abnormal metabolite produced in tyrosinemia, is a potent inhibitor of the activity of ALA dehydratase, it has a far less effect on the synthesis of the enzyme protein.

The specific activities of peroxidase and aminolevulinic acid dehydratase during the growth cycle of peanut suspension culture

1976 ◽  
Vol 54 (18) ◽  
pp. 2089-2094 ◽  
Author(s):  
V. C. Kossatz ◽  
R. B. van Huystee
Keyword(s):  
Suspension Culture ◽  
Protein Content ◽  
Aminolevulinic Acid ◽  
Specific Activity ◽  
Growth Cycle ◽  
Acid Dehydratase ◽  
Green Tissue ◽  
Porphobilinogen Synthase ◽  
Dehydratase Activity ◽  
Ala Dehydratase

Peroxidase (EC 1.11.1.7) enzyme units that were recovered by sequential extraction at low and high ionic strength buffer pH 7 from a peanut suspension culture at various intervals of cell growth appeared to increase with culture time. In particular, at the end of a 14-day growth cycle, peroxidase specific activity rose while protein content and the specific activity of porphobilinogen synthase (aminolevulinic acid, dehydratase EC 4.2.1.24) declined. The decrease of the protein content could probably be accounted for by the 95% decrease of protein synthesis at the end of the growth phase. The highest specific activity of aminolevulinic acid dehydratase (ALA dehydratase) appeared to be associated with organelles which could be precipitated at 500 × g and this specific activity appeared to be unaffected by the stage of growth of these cells. It is suggested that the ALA dehydratase activity in nonchlorophyllous peanut cells, which is as high as that found in green tissue, may play a function in the biosynthesis of the hemoprotein peroxidase.

scholarly journals The role of the erythroid-specific delta-aminolevulinate synthase gene expression in erythroid heme synthesis

Blood ◽  
1995 ◽  
Vol 86 (3) ◽  
pp. 940-948 ◽  
Author(s):  
K Meguro ◽  
K Igarashi ◽  
M Yamamoto ◽  
H Fujita ◽  
S Sassa
Keyword(s):  
Gene Expression ◽  
Mrna Level ◽  
Mrna Levels ◽  
Beta Globin ◽  
Aminolevulinate Synthase ◽  
Heme Synthesis ◽  
Murine Erythroleukemia ◽  
Erythroid Development ◽  
Ala Dehydratase

Abstract Using antisense technology, the effects of suppressed gene expression of the erythroid-specific delta-aminolevulinate (ALA) synthase (ALAS-E) on heme synthesis, expression of mRNAs encoding an erythroid-specific transcription factor NF-E2, other heme pathway enzymes, and beta-globin were examined in murine erythroleukemia (MEL) cells. In MEL cells in which an antisense ALAS-E RNA was expressed (AS clone), sense ALAS-E mRNA levels in both untreated and dimethylsulfoxide (DMSO)-treated cells were decreased compared with their respective controls. Heme synthesis in AS clones was decreased in proportion to the suppressed levels of ALAS-E mRNA. In addition, mRNAs for ALA dehydratase, porphobilinogen deaminase, ferrochelatase (FeC), and beta-globin were also decreased in AS clones. There was a strong correlation between the level of ALAS-E mRNA and most of the mRNAs of the heme pathway enzymes and beta-globin. There was a decrease in the mRNA level of p45, but not of mafK, which are the large and the small subunits of NF-E2, respectively, in AS clones. Treatment of AS cells with hemin and ALA in the presence of DMSO partially restored the suppressed mRNA levels for beta-globin and FeC and heme content, respectively. These findings thus indicate that heme formation, which is determined by the level of ALAS- E, plays an essential role on gene expression of many proteins necessary for erythroid development.

delta-Aminolevulinate dehydratase in human erythroleukemia cells: an immunologically distinct enzyme

Blood ◽  
1985 ◽  
Vol 65 (4) ◽  
pp. 939-944 ◽  
Author(s):  
CS Chang ◽  
S Sassa
Keyword(s):  
Butyric Acid ◽  
Deae Cellulose ◽  
K562 Cells ◽  
Normal Adult ◽  
Erythroleukemia Cells ◽  
Normal Enzyme ◽  
Normal Human ◽  
Dehydratase Activity ◽  
Ala Dehydratase ◽  
Selenium Oxide

Abstract Physicochemical and immunologic properties of delta-aminolevulinate (ALA) dehydratase in human K562 erythroleukemia cells were examined. ALA dehydratase activity was found to increase in K562 cells after treatment with butyric acid or selenium oxide. Enzyme activity in untreated K562 cells was comparable to that in normal adult erythrocytes but was increased three- to six-fold in K562 cells treated with 1.2 mmol/L butyric acid or 0.03 mmol/L selenium oxide. The Michaelis-Menten constant (Km), the inhibitor constant (Ki), and elution profile by diethylaminoethyl (DEAE) cellulose chromatography were similar for ALA dehydratase from K562 cells and normal human adult and human fetal erythrocytes. However, ALA dehydratase from K562 cells did not react with a monospecific rabbit antibody against ALA dehydratase purified from normal adult erythrocytes, although the antibody reacted with the enzyme from normal adult and fetal red cells. These findings indicate that ALA dehydratase in K562 cells is immunologically distinct from the normal enzyme.

ALA-Dehydratase Activation by Zinc

Enzyme ◽  
1971 ◽  
Vol 12 (6) ◽  
pp. 708-710 ◽  
Author(s):  
M. Abdulla ◽  
Birgitta Haeger-Aronsen
Keyword(s):  
Ala Dehydratase
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