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Cyclic activity of L‐asparaginase through reversible phosphorylation in Leptosphaeria michotii
Author(s) -
Jerebzoff Stéphan,
Jerebzoff-Quintin Simonne
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80461-5
Subject(s) - dephosphorylation , phosphorylation , asparaginase , chemistry , phosphatase , enzyme , specific activity , in vitro , enzyme assay , biochemistry , protein kinase a , alkaline phosphatase , microbiology and biotechnology , biology , leukemia , immunology , lymphoblastic leukemia
Asparaginase in L. michotii has previously been shown to have an activity rhythm, the mechanisms of which were investigated. In vitro activation, or reactivation after dephosphorylation, of the partially (200‐fold) purified asparaginase with protein kinase activity was obtained by ATP or P i addition; these effects varied according to the phase of the activity rhythm at which enzyme was extracted. A high‐ M r aggregate with asparaginase activity was phosphorylated by [γ‐ 32 P]ATP. By SDS‐electrophoresis of dephosphorylated asparaginase a ∼60‐kDa 32 P‐labelled protein with alkaline phosphatase activity became detectable. Regulation of the asparaginase activity rhythm in L. michotii is dependent on a reversible phosphorylation process.