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Quinolinic acid phosphoribosyltransferase (EC 2.4.2.19) was purified 3600-fold from rat liver and 280-fold from rat brain. Kinetic analyses (Km = 12 microM for the substrate quinolinic acid and Km = 23 microM for the cosubstrate phosphoribosylpyrophosphate), physicochemical properties of the purified enzymes, inhibition by phthalic acid (Ki = 1.4 microM) and molecular weight determination (Mr 160 000 for the holoenzyme, consisting of five identical 32 kDa subunits) indicated the structural identity of quinolinic acid phosphoribosyltransferase from the two rat tissues. This was further confirmed immunologically, using antibodies raised against purified rat liver quinolinic acid phosphoribosyltransferase. Rat quinolinic acid phosphoribosyltransferase differs in several aspects from quinolinic acid phosphoribosyltransferase isolated from other organisms. The purified enzyme will prove a useful tool in the examination of a possible role of quinolinic acid in cellular function and/or dysfunction.
E Okuno, and
R Schwarcz
February 1985,
Journal of neurochemistry,
E Okuno, and
R Schwarcz
November 1974,
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E Okuno, and
R Schwarcz
April 2006,
Proteins,
E Okuno, and
R Schwarcz
June 1985,
Brain research,
E Okuno, and
R Schwarcz
March 1975,
Biochimica et biophysica acta,
E Okuno, and
R Schwarcz
January 1991,
Advances in experimental medicine and biology,
E Okuno, and
R Schwarcz
January 1978,
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E Okuno, and
R Schwarcz
December 1949,
The Journal of biological chemistry,
E Okuno, and
R Schwarcz
January 1993,
Journal of neurochemistry,
E Okuno, and
R Schwarcz
February 1974,
Biochemical and biophysical research communications,
