Isolation of a cDNA for rat brain glutaminase.
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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Laboratory of Molecular Biology, NINCDS, Bethesda, MD 20892.
Hwang
J J
JJ
Shapiro
R A
RA
Wenthold
R J
RJ
Nakatani
Y
Y
Lampel
K A
KA
Thomas
J W
JW
Huie
D
D
Curthoys
N P
NP
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology*; D004247:DNA / Q000032:analysis / Q000302:isolation & purification*; D005972:Glutaminase / Q000032:analysis / Q000235:genetics*; D007118:Immunoassay; D007668:Kidney / Q000201:enzymology; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains
D004247:DNA; D005972:Glutaminase