Les isophosphatases alcalines d' Escherichia coli. Séparation, propriétés cinétiques et structurales
1967; Elsevier BV; Volume: 147; Issue: 2 Linguagem: Inglês
10.1016/0005-2795(67)90406-0
ISSN1878-1454
AutoresClaude Lazdunski, Michel Lazdunski,
Tópico(s)Erythrocyte Function and Pathophysiology
ResumoPurification, kinetic and structural properties of the alkaline isophosphatases of Escherichia coli The alkaline phosphatase of Escherichia coli (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) is heterogeneous on disc and starch-gel electrophoresis. Three isophosphatases were separated on a DEAE-cellulose column. These isozymes, which are formed in vivo, are dimers, two of them AA and BB are composed of two identical subunits, the third AB is a hybrid containing one monomer of each type. The subunits have similar amino acid compositions. Several kinetic and structural properties of the isozymes were studied and found to be similar.
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