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从小鼠脑培养的神经元和星形胶质细胞中的谷氨酰胺酶:动力学特性以及磷酸盐、谷氨酸和氨的影响。

Glutaminase in neurons and astrocytes cultured from mouse brain: kinetic properties and effects of phosphate, glutamate, and ammonia.

作者信息

Hogstad S, Svenneby G, Torgner I A, Kvamme E, Hertz L, Schousboe A

机构信息

Neurochemical Laboratory, University of Oslo, Norway.

出版信息

Neurochem Res. 1988 Apr;13(4):383-8. doi: 10.1007/BF00972489.

Abstract

Phosphate activated glutaminase comprises two kinetically distinguishable enzyme forms in cultures of cerebellar granule cells, of cortical neurons and of astrocytes. Specific activity of glutaminase is higher in cultured neurons compared with astrocytes. Glutaminase is activated by phosphate in all cell types investigated, however, glutaminase in astrocytes requires a much higher concentration of phosphate for half maximal activation. One of the products, glutamate, inhibits the enzyme strongly, whereas the other product ammonia has only a slight inhibitory action on the enzyme.

摘要

在小脑颗粒细胞、皮层神经元和星形胶质细胞培养物中,磷酸激活型谷氨酰胺酶包含两种动力学上可区分的酶形式。与星形胶质细胞相比,培养的神经元中谷氨酰胺酶的比活性更高。在所有研究的细胞类型中,谷氨酰胺酶都被磷酸盐激活,然而,星形胶质细胞中的谷氨酰胺酶需要高得多的磷酸盐浓度才能达到半数最大激活。其中一种产物谷氨酸对该酶有强烈抑制作用,而另一种产物氨对该酶只有轻微抑制作用。

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