Jerebzoff S, Jerebzoff-Quintin S
FEBS Lett. 1984 Jun 4;171(1):67-71. doi: 10.1016/0014-5793(84)80461-5.
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 Pi addition; these effects varied according to the phase of the activity rhythm at which enzyme was extracted. A high-Mr aggregate with asparaginase activity was phosphorylated by [gamma-32P]ATP. By SDS-electrophoresis of dephosphorylated asparaginase a approximately 60-kDa 32P-labelled protein with alkaline phosphatase activity became detectable. Regulation of the asparaginase activity rhythm in L. michotii is dependent on a reversible phosphorylation process.
先前已表明米氏链霉菌中的天冬酰胺酶具有活性节律，并对其机制进行了研究。通过添加ATP或Pi，可实现对部分（200倍）纯化的具有蛋白激酶活性的天冬酰胺酶进行体外激活或去磷酸化后的再激活；这些效应根据提取酶时的活性节律阶段而有所不同。具有天冬酰胺酶活性的高分子量聚集体被[γ-32P]ATP磷酸化。通过对去磷酸化的天冬酰胺酶进行SDS电泳，可检测到一种具有碱性磷酸酶活性的约60 kDa的32P标记蛋白。米氏链霉菌中天冬酰胺酶活性节律的调节依赖于一个可逆的磷酸化过程。
