Purification and properties of human erythrocyte delta-amino-levulinic acid dehydratase (EC 4-2-1-24).

Abstract:

:Human delta-aminolevulinic acid dehydratase (ALA-D) was purified 9 000-fold by salt precipitation, ion-exchange chromatography and gel filtration. These methods resulted into an electrophoretically and immunologically pure protein. The optimum pH of the enzyme is 6.6 and its Km with ALA : 4.8 X 10(-4) M. The enzymatic activity was increased by thiol-containing substances, such as dithiothreitol (DTT), which protect the -SH groups of the protein. Zinc, a portion of the enzyme molecule, was partly lost during the purification procedure; its addition enhances the enzymatic activity. Determination of molecular weights and electron microscopy study are in favor of an octameric structure.

journal_name

Biochimie

journal_title

Biochimie

authors

Despaux N,Comoy E,Bohuon C,Boudène C

doi

10.1016/s0300-9084(80)80256-2

subject

Has Abstract

pub_date

1979-01-01 00:00:00

pages

1021-8

issue

9

eissn

0300-9084

issn

1638-6183

journal_volume

61

pub_type

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