|
|
||||||||
Clinical Chemistry, Vol 20, 1287-1291, Copyright © 1974 by the American Association for Clinical Chemistry
1 Department of Public Health, Okayama University Medical
School, Okayama, Japan.
I describe a new method for measurement of aminolaevulinate dehydratase (EC 4.2.1.24) activity of human erythrocytes. In this method, the amount of substrate
-aminolevulinic acid consumed (instead of the amount
of porphobilinogen formed) is determined colorimetrically. In the incubation mixture, the
-aminolevulinic acidpyrrole produced by the condensation of
-aminolevulinic acid with ethyl acetoacetate is separated from porphobilinogen by extraction with ethyl acetate, without
resorting to ion-exchange column chromatography. The
pyrrole-containing extract is treated with a modified
Ehrlich's reagent. Activity of the enzyme is expressed
as micromoles of
-aminolevulinic acid consumed per
minute per liter of erythrocytes. Enzyme activity is more
accurately estimated by the present method than by the
usual method in which porphobilinogen is measured.
-aminolevulinic acid colorimetry normal values porphobilinogen inhibition
of enzymatic activity toxicology of lead screening
Submitted on July 1, 1974
Accepted on July 29, 1974
The following articles in journals at HighWire Press have cited this article:
![]() |
A Diouf, G Garc'on, C Thiaw, Y Diop, M Fall, B Ndiaye, T Siby, M H Hannothiaux, F Zerimech, D Ba, et al. Environmental lead exposure and its relationship to traffic density among Senegalese children: a pilot study Human and Experimental Toxicology, October 1, 2003; 22(10): 559 - 564. [Abstract] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |