Reiss P M, Pierce S K, Bishop S H
J Exp Zool. 1977 Nov;202(2):253-7. doi: 10.1002/jez.1402020215.
Glutamate dehydrogenase (E.C. 14.1.3) was localized in the mitochondria from heart, gill, mantle and hepatopancreas of this euryhaline bivalve mollusc. Activity levels were low (0.1-0.4 mumoles/min/g wet weight) in all tissues when assayed in the glutamate forming direction. Partially purified gill mitochondrial GDH was most active at pH 8.5. The rate in the glutamate deaminating direction was 10-20% of the rate in the glutamate forming direction. ADP at apparent Ka concentrations of micrometer (glutamate formation) and 170 micrometer (glutamate deamination) enhanced GDH activity, 8- and 4-fold respectively. GDH, in vivo, is probably in the activated form and appears to function in glutamate synthesis rather than ammonia formation. However, based on the low activities obtained, the role of GDH in salinity induced amino acid synthesis seems minimal.
谷氨酸脱氢酶（E.C. 14.1.3）定位于这种广盐性双壳贝类软体动物的心脏、鳃、外套膜和肝胰腺的线粒体中。当以谷氨酸生成方向进行测定时，所有组织中的活性水平都很低（0.1 - 0.4微摩尔/分钟/克湿重）。部分纯化的鳃线粒体GDH在pH 8.5时活性最高。谷氨酸脱氨方向的速率是谷氨酸生成方向速率的10 - 20%。在微摩尔级的表观Ka浓度（谷氨酸生成）和170微摩尔（谷氨酸脱氨）下，ADP分别使GDH活性提高了8倍和4倍。在体内，GDH可能处于活化形式，似乎在谷氨酸合成而非氨生成中发挥作用。然而，基于所获得的低活性，GDH在盐度诱导的氨基酸合成中的作用似乎很小。
