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D-aminolevulinate

ALA, ALA-D = aminolevulinic acid dehydrase NCV = nerve conduction velocity... [Pg.370]

Dieter, M.P. and M.T. Finley. 1978. Erythrocyte d-aminolevulinic acid dehydratase activity in mallard ducks duration of inhibition after lead shot dosage. Jour. Wild . Manage. 42 621-625. [Pg.329]

Hayashi, M. 1983. Lead toxicity in the pregnant rat. I. The effect of high-level lead on d-aminolevulinic acid dehydratase activity in maternal and fetal blood or tissues. Environ. Res. 30 152-160. [Pg.332]

Schmitt, C.J., F.J. Dwyer, and S.E. Finger. 1984. Bioavailability of Pb and Zn from mine tailings as indicated by erythrocyte d-aminolevulinic acid dehydratase (ALA-D) activity in suckers (Pisces Catostomidae). Canad. Jour. Fish. Aquat. Sci. 41 1030-104). [Pg.341]

Scheme 4. The heme biosynthetic pathway. In vivo administration of d-aminolevulinic acid induces accumulation of fluorescent protoporphyrin IX (PpIX) preferably in malignant tissues... Scheme 4. The heme biosynthetic pathway. In vivo administration of d-aminolevulinic acid induces accumulation of fluorescent protoporphyrin IX (PpIX) preferably in malignant tissues...
If the heme is not utilized in heme proteins, heme and hematin both inhibit and decrease the synthesis of d-aminolevulinate, the first unique intermediate in heme synthesis. [Pg.570]

The biosynthesis of porphyrin involves the formation of porphobilinogen from two molecules of S-aminolevulinic acid. The precise mechanism for this biosynthesis is as yet unknown. A possible mechanism starts with the formation of an imine between the enzyme that catalyzes the reaction and one of the molecules of S-aminolevulinic acid. An aldol-type condensation occurs between the imine and a free molecule of d-aminolevulinic acid. Nucleophilic attack by the amino group on the imine closes the ring. The enzyme is then eliminated, and removal of a proton creates the aromatic ring. [Pg.910]

Keiada SM, Shelton E, Kaufmann RB and Khouey MJ (2001) d-Aminolevulinic acid dehydratase genotype and lead toxicity A HuGE Review. Am J Epidemiol 154 1-13. [Pg.473]

Beegdahl 1A, Geubb A, Schutz A, Desnick RJ, Wetmue JG, Sassa S and Skeeeving S (1997). Lead-binding to d-aminolevulinic acid dehydratase (ALAD) in human erythrocytes. Pharmacol Toxicol 81 153-158. [Pg.896]

Schutz a and Skerfving S (1976) Effect of a short, heavy exposure to lead dust upon blood lead level, erythrocyte d-aminolevulinic acid dehydratase activity and urinary excretion lead, d-aminolevu-linic acid, and coproporphyrine. Scand J Work Environ Health 1 54-59. [Pg.899]

Hematological effects Decreased heme biosynthesis by inhibiting d-aminolevulinic acid dehydratase (ALAD) and ferrochelatase activity, an increase in blood and plasma d-aminolevulinic acid (ALA) and free erythrocyte protoporphyrins, hemolytic anemia and Frank anemia... [Pg.294]

Mauzerall, D., and S. Granick. "The Occurrence and Determination of d-Aminolevulinic Acid and Propho-bilinogen in Urine." Journal of Biological Chemistry, 219 1956,435-446. [Pg.318]


See other pages where D-aminolevulinate is mentioned: [Pg.240]    [Pg.247]    [Pg.142]    [Pg.329]    [Pg.170]    [Pg.217]    [Pg.299]    [Pg.161]    [Pg.329]    [Pg.751]    [Pg.144]    [Pg.197]    [Pg.149]    [Pg.173]    [Pg.155]    [Pg.171]    [Pg.128]    [Pg.361]    [Pg.141]    [Pg.209]    [Pg.76]    [Pg.115]    [Pg.173]    [Pg.170]    [Pg.177]    [Pg.193]    [Pg.259]    [Pg.910]    [Pg.453]    [Pg.269]    [Pg.29]    [Pg.438]    [Pg.192]    [Pg.48]   
See also in sourсe #XX -- [ Pg.438 , Pg.439 ]




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