Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Reevaluation of a sensitive indicator of early lead exposure. Measurement of porphobilinogen synthase in blood.

Literature DB >> 1713045

Reevaluation of a sensitive indicator of early lead exposure. Measurement of porphobilinogen synthase in blood.

Abstract

A principal target for the environmental toxin lead (Pb) is porphobilinogen synthase (PBGS), a Zn-metalloenzyme necessary for heme biosynthesis. Measurement of blood Pb inhibited PBGS is the most sensitive indicator of subclinical Pb intoxication, but problems with the assay have diminished its use. This report identifies Pb as a slow acting inhibitor of PBGS. The activity of PBGS could change up to sixfold during an hourlong clinical assay of Pb contaminated blood, and activity is profoundly effected by the presence of serum proteins, such as albumin. When PBGS catalyzed PBG production is allowed to reach a steady state rate, kinetic data on purified PBGS support the hypothesis that Pb inhibition of PBGS results from direct substitution for Zn.

Entities: Chemical Gene

Mesh：

Substances：

Year: 1991 PMID： 1713045 DOI： 10.1007/bf02990469

Source DB: PubMed Journal: Biol Trace Elem Res ISSN： 0163-4984 Impact factor: 3.738

21 in total

1. In vitro pyrrole and porphyrin synthesis in lead poisoning and iron deficiency.

Authors: H C LICHTMAN; F FELDMAN
Journal: J Clin Invest Date: 1963-06 Impact factor: 14.808

2. Increased lead absorption and lead poisoning in young children. A statement by the Center for Disease Control.

Authors:
Journal: J Pediatr Date: 1975-11 Impact factor: 4.406

3. Subclinical lead exposure in philadelphia schoolchildren. Identification by dentine lead analysis.

Authors: H L Needleman; I Davidson; E M Sewell; I M Shapiro
Journal: N Engl J Med Date: 1974-01-31 Impact factor: 91.245

4. Stability constant for the zinc-dithiothreitol complex.

Authors: N W Cornell; K E Crivaro
Journal: Anal Biochem Date: 1972-05 Impact factor: 3.365

5. Erythrocytic aminolevulinic acid dehydratase (ALAD) activity as a biologic parameter for determining exposures to lead.

Authors: D H Goldstein; T J Kneip; V P Rulon; N Cohen
Journal: J Occup Med Date: 1975-03

6. Purification and properties of 5-aminolaevulinate dehydratase from human erythrocytes.

Authors: P N Gibbs; A G Chaudhry; P M Jordan
Journal: Biochem J Date: 1985-08-15 Impact factor: 3.857

7. The role of zinc with special reference to the essential thiol groups in delta-aminolevulinic acid dehydratase of bovine liver.

Authors: I Tsukamoto; T Yoshinaga; S Sano
Journal: Biochim Biophys Acta Date: 1979-09-12

2. Metals control activity and expression of the heme biosynthesis enzyme delta-aminolevulinic acid dehydratase in Bradyrhizobium japonicum.

Authors: S Chauhan; D E Titus; M R O'Brian
Journal: J Bacteriol Date: 1997-09 Impact factor: 3.490

Reevaluation of a sensitive indicator of early lead exposure. Measurement of porphobilinogen synthase in blood.

1. In vitro pyrrole and porphyrin synthesis in lead poisoning and iron deficiency.

2. Increased lead absorption and lead poisoning in young children. A statement by the Center for Disease Control.

3. Subclinical lead exposure in philadelphia schoolchildren. Identification by dentine lead analysis.

4. Stability constant for the zinc-dithiothreitol complex.

5. Erythrocytic aminolevulinic acid dehydratase (ALAD) activity as a biologic parameter for determining exposures to lead.

6. Purification and properties of 5-aminolaevulinate dehydratase from human erythrocytes.

7. The role of zinc with special reference to the essential thiol groups in delta-aminolevulinic acid dehydratase of bovine liver.

8. Interferences in the delta-aminolevulinic acid dehydratase (ALA-D) assay.

9. Investigation of the effect of metal ions on the reactivity of thiol groups in human 5-aminolaevulinate dehydratase.

10. In vivo regulation of delta-aminolevulinate dehydratase activity.

1. Delta-ALAD activity variations in red blood cells in response to lead accumulation in rock doves (Columba livia).

2. Metals control activity and expression of the heme biosynthesis enzyme delta-aminolevulinic acid dehydratase in Bradyrhizobium japonicum.

3. The morpheein model of allostery: evaluating proteins as potential morpheeins.

Review 4. Porphobilinogen synthase, the first source of heme's asymmetry.

Review 5. Influence of the common human delta-aminolevulinate dehydratase polymorphism on lead body burden.