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1. Hypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8) from Saccharomyces cerevisiae was purified 9400-fold by affinity chromatography giving rise to an electrophoretically homogeneous preparation. 2. The molecular weight of the enzyme was determined by gel filtration with Sephadex G-100 and by sodium dodecylsulfate gel electrophoresis. Both methods reveal a molecular weight of 51,000. 3. The enzyme requires Mg2+ and has its pH optimum at 8.5. 4. Isoelectric focussing as well as gel electrophoresis of the purified extract reveals a single band which exhibits enzyme activity. The isoelectric point of the enzyme is 5.1. 5. The enzyme displays Michaelis-Menten kinetics with apparent Michaelis constants for hypoxanthine, guanine and phosphoribosylpyrophosphate of 23 microns, 18 microns, and 50 microns respectively.
R Schmidt, and
H Wiegand, and
U Reichert
August 1981,
Biochemistry,
R Schmidt, and
H Wiegand, and
U Reichert
January 1983,
Molecular & general genetics : MGG,
R Schmidt, and
H Wiegand, and
U Reichert
June 1977,
European journal of biochemistry,
R Schmidt, and
H Wiegand, and
U Reichert
January 1975,
The Journal of biological chemistry,
R Schmidt, and
H Wiegand, and
U Reichert
March 1989,
Molecular and biochemical parasitology,
R Schmidt, and
H Wiegand, and
U Reichert
December 2003,
Protein expression and purification,
R Schmidt, and
H Wiegand, and
U Reichert
January 1973,
Advances in experimental medicine and biology,
R Schmidt, and
H Wiegand, and
U Reichert
September 1997,
Biochimica et biophysica acta,
R Schmidt, and
H Wiegand, and
U Reichert
June 1974,
Tropenmedizin und Parasitologie,
R Schmidt, and
H Wiegand, and
U Reichert
September 1980,
The Journal of investigative dermatology,
