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Am J Physiol Cell Physiol 279: C648-C657, 2000;
0363-6143/00 $5.00
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Vol. 279, Issue 3, C648-C657, September 2000

Properties and submitochondrial localization of pig and rat renal phosphate-activated glutaminase

Bjørg Roberg1, Ingeborg A. Torgner1, Jon Laake2,3, Yutaka Takumi2,4, Ole P. Ottersen2, and Elling Kvamme1

1 Neurochemical Laboratory, Domus Medica, University of Oslo, 0317 Oslo; 2 Department of Anatomy, Domus Medica, University of Oslo, N-0317 Oslo; 3 Anestesiavd., Rogaland Sentralsykehus, 4003 Stavanger, Norway; and 4 Department of Otorhinolaryngology, Hirosaki University School of Medicine, 5, Zaifu-cho, Hirosaki, Japan.

Two pools of phosphate-activated glutaminase (PAG) were separated from pig and rat renal mitochondria. The partition of enzyme activity corresponded with that of the immunoreactivity and also with the postembedding immunogold labeling of PAG, which was associated partly with the inner membrane and partly with the matrix. The outer membrane was not labeled. PAG in intact mitochondria showed enzymatic characteristics that were similar to that of the membrane fraction and also mimicked that of the polymerized form of purified pig renal PAG. PAG in the soluble fraction showed properties similar to that of the monomeric form of purified enzyme. It is indicated that the pool of PAG localized inside the inner mitochondrial membrane is dormant due to the presence of high concentrations of the inhibitor glutamate. Thus the enzymatically active PAG is assumed to be localized on the outer face of the inner mitochondrial membrane. The activity of this pool of PAG appears to be regulated by compounds in the cytosol, of which glutamate may be most important.

mitochondria; mitochondrial inner membrane; immunoelectron microscopy


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