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THE INHIBITION EFFECTS OF DIFFERENT LEAD CONCENTRATIONS ON ALA‐D ACTIVITY AND RECOVERY EFFECTS OF HIGHER TEMPERATURES ON INHIBITED ALA‐D ACTIVITY ON HUMAN BLOOD
Author(s) -
SAHITI HAZBIJE BOJNIKU,
ELEZAJ ISA REXHEP,
SELIMI QERIM ISAK,
LETAJ KASUM RRUSTEM,
MEHMETI SADIK IDRIZ
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.lb106-c
Subject(s) - chemistry , in vivo , allosteric regulation , in vitro , human blood , lead (geology) , enzyme , enzyme assay , pharmacology , biochemistry , biology , physiology , paleontology , microbiology and biotechnology
The inhibition effects of different lead concentrations (2–100 μg/dl) on ALA‐D activity (E.C. 4.2.1.24), and recovery effects of higher temperatures (37, 42, 50 and 60 °C/60 min.), on inhibited ALA‐D activity (in vitro) in human blood were analyzed. The negative correlation (r =‐ 0.799) was estimated between Pb concentration and ALA‐D activity from 2–10 μg/dl in temperature of 37 °C. The ALA‐D activity in the blood hemolysate with a same Pb concentrations in temperatures of 42, 50 and 60 °C were significantly higher in comparison with that on 37 °C. The ALA‐D activity of blood with Pb concentration from 20–100 μg/dl at 37 ° was significantly inhibited in comparison with ALA‐D activity with the same Pb‐concentration incubated in 42, 50 and 60 °C /60 min. The recovery effect was prominently expressed on 60 °C. In relation to this point, an allosteric type of inhibition would offer a plausible explanation. These changes would prevent lead from interfering with the active center of the enzyme. This hypothesis seems to gain support from the fact that the inhibition caused by lead in vivo can be almost completely restored by heating.