Abstract
Hypoxanthine-guanine phosphoribosyltransferase (HGPR transferase) (EC 2.4.2.8) has been purified approximately 4500-fold to apparent homogeneity from mouse liver. The procedure involves the use of affinity chromatography and was designed to be readily adaptable to small scale isolations. The enzyme appears to be composed of 3 subunits of identical molecular weight (27,000 per subunit). The subunit molecular weight has also been determined by the analysis of radioactively labeled HGPR transferase immunoprecipitated from wild type and mutant (HGPR transferase) mouse tissue culture cell lines.
Highlights
Was designed to be readily adaptable to small scale isolations
HGPR transferase was isolated from mouse liver rather than mouse L cells grown in culture
The studies reported here show that the enzyme from L cells and mouse liver have identical subunit molecular weights and sedi
Summary
Hypoxanthine-guanine phosphoribosyltransferase (HGPR transferase) (EC 2.4.2.8) has been purified approximately. The enzyme appears to be composed of 3 subunits of identical molecular weight (27,000 per subunit). The subunit molecular weight has been determined by the analysis of radioactively labeled HGPR transferase immunoprecipitated from wild type and mutant (HGPR transferase) mouse tissue culture cell lines. Our interest in the enzyme arose from the possibility of using this system for the isolation of nonsense suppressor mutants. HGPR transferase was isolated from mouse liver rather than mouse L cells grown in culture. The studies reported here show that the enzyme from L cells and mouse liver have identical subunit molecular weights and sedi-. The sedimentation coefficient in sucrose gradients is 5 S These data are most compatible with the assignment of a molecular weight of approximately. HGPR transferase has greatly simplified the rapid purification of this enzyme
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