JBC, Vol. 252, Issue 6, 2082-2088, Mar, 1977
Purification and characterization of UDP-galactose-4-epimerase from bovine tissues
C. R. Geren and K. E. Ebner
Bovine liver and mammary UDP-galactose-4-epimerases have been purified to
apparent electrophoretic homogeneity by a simple procedure involving the
use of two affinity adsorbants, UDP-hexanolamine-Sepharose and
NAD+-hexanolamine-Sepharose. The bovine thyroid epimerase has been
partially purified by the same procedure. All three enzymes require NAD+
for activity, and all have a similar apparent molecular weight of
approximately 40,000 as determined by gel filtration of the active enzymes.
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the liver and
mammary epimerases revealed similar molecular weights of 37,000 for both
enzymes thus indicating that neither protein was dimeric. During
development of the isolation procedure conditions were determined which
would stabilize enzymatic activity in very dilute solutions. The liver and
mammary enzymes, although similar in some respects, differed in amino acid
composition and specific activity.
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