Abstract
Quinolinate phosphoribosyltransferase (an intermediary enzyme in the de novo NAD biosynthetic pathway) was purified and crystallized for the first time from mammalian tissue. The crystalline preparation was certified to be homogeneous by ultracentrifugal analysis and polyacrylamide gel disc electrophoresis. The molecular weight of this enzyme protein was calculated as 172,000 with the sedimentation velocity method and as 173,000 using gel permeation chromatography on Sephadex G-200. The polypeptide chain molecular weight of this enzyme protein was calculated as 34,000 using the dodecyl sulfate-polyacrylamide gel electrophoresis and as 35,000 with the sedimentation equilibrium method. Quinolinate phosphoribosyltransferase from hog liver may consist of five identical subunits.
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