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JBC, Vol. 250, Issue 1, 120-126, Jan, 1975
S. H. Hughes, G. M. Wahl and M. R. Capecchi
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.
Purification and characterization of mouse hypoxanthine-guanine phosphoribosyltransferase
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G. Johnson, L. Eisenberg, and B. Migeon Human and mouse hypoxanthine-guanine phosphoribosyltransferase: dimers and tetramers Science, January 12, 1979; 203(4376): 174 - 176. [Abstract] [PDF] |
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