Abstract
The product, N-acetyl-D-mannosamine is determined by a modification of the Morgan–Elson procedure. With the purified enzyme, uridine diphosphate (UDP), can be determined by coupling the reaction with nueleotide diphosphokinase, PEP, lactic dehydrogenase, and reduced diphosphopyridine nucleotide (DPNH). A unit of enzyme is the quantity that produces 1.0 micromole of N-acetyl-D-mannosamine in 20 minutes under the conditions described. Specific activity is defined as the units of enzyme per milligram of protein. The enzyme is specific for UDP-N-acetylglucosamine. UDP-glucose, N-acetyl-D-glucosamine, N-acetyl-D-glucosamine 1-phosphate, and UDP-N-acetylgalactosamine are inactive. The purified enzyme is extremely unstable, often losing all activity within a few hours, and it is therefore advisable to carry out the entire purification procedure at one time. The enzyme shows maxima of activity at pH 7.7 with Tris-HCl buffer and pH 6.7 using imidazole buffer. A double peak encompassing these two optima is observed when Tris-maleate buffer is used over the entire pH range.
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