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
Biochimiejournal_title
Biochimieauthors
Despaux N,Comoy E,Bohuon C,Boudène Cdoi
10.1016/s0300-9084(80)80256-2subject
Has Abstractpub_date
1979-01-01 00:00:00pages
1021-8issue
9eissn
0300-9084issn
1638-6183journal_volume
61pub_type
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