Akimova N I, Evstigneeva Z G, Kretovich V L
Biokhimiia. 1977 May;42(5):947-51.
A decrease of glutamine synthetase (E. C. 6.3.1.2.) activity was observed under the assimilation of ammonium nitrogen in Chlorella. At the same time a decrease of ATP content in Chlorella cells took place. The ATP content was 7-fold decreased, while ADP and AMP contents were 4-fold and 3-fold increased respectively, after 15 min. of Chlorella incubation on "ammonium" medium. Further incubation for 45 min, resulted in gradual increase of ATP content and in decrease of ADP and AMP contents. The value of energy charge in ammonium assimilating Chlorella cells sharply decreased for first 15 min. of incubation and then it normalized gradually. The experiments with glutamine synthetase preparation, isolated from ammonium assimilating cells, have shown that ADP and AMP are strong inhibitors of the enzyme in the presence of Mg2+, and only ADP produces the inhibitory effect in the presence of Mn2+. No enzyme reactivation was observed after the transfer of ammonium assimilating cells into nitrogen-free medium or nitrate medium, the enzyme activity increasing at the expense of enzyme protein synthesis denovo.
在小球藻同化铵态氮的过程中,观察到谷氨酰胺合成酶(E.C.6.3.1.2.)的活性下降。与此同时,小球藻细胞中的ATP含量也下降。在“铵”培养基上培养小球藻15分钟后,ATP含量下降了7倍,而ADP和AMP含量分别增加了4倍和3倍。进一步培养45分钟后,ATP含量逐渐增加,ADP和AMP含量下降。在铵同化小球藻细胞中,能量电荷值在培养的前15分钟急剧下降,然后逐渐恢复正常。用从铵同化细胞中分离出的谷氨酰胺合成酶制剂进行的实验表明,在Mg2+存在下,ADP和AMP是该酶的强抑制剂,而在Mn2+存在下只有ADP产生抑制作用。将铵同化细胞转移到无氮培养基或硝酸盐培养基后,未观察到酶的重新激活,酶活性通过从头合成酶蛋白而增加。