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. 1988 Jun;427(3):247-54.
doi: 10.1016/0169-328x(88)90047-2.

Isolation of a cDNA for rat brain glutaminase

C Banner  1 , J J Hwang, R A Shapiro, R J Wenthold, Y Nakatani, K A Lampel, J W Thomas, D Huie, N P Curthoys
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Isolation of a cDNA for rat brain glutaminase

C Banner et al. Brain Res. 1988 Jun.

Abstract

A single phage was isolated from a lambda gt11 rat brain cDNA library by screening with antibodies prepared against rat renal glutaminase. Partial proteolysis of the fusion protein produced by a lysogen of the isolated phage generated a series of immunoreactive peptides that co-migrated with those derived from the purified brain glutaminase. The cDNA has a single open reading frame which encodes 326 amino acids that are in frame with beta-galactosidase. A 72-kDa protein, corresponding in size to the precursor of mitochondrial glutaminase, was immunoprecipitated from the translation products of rat renal mRNA that selectively hybridized to the cDNA. A probe made from the glutaminase cDNA detected an mRNA about 6 kb in length. This mRNA was present in rat brain and normal kidney RNA, increased 6-fold in acidotic kidney RNA, but was not detectable in liver RNA.

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