Characterization and purification of AMP deaminase from pork

An AMPD was purified from fresh pork by following procedures:Cellulose phosphate chromatography, Q -Sepharose Fast Flow chromatography and 5’-AMP Sepharose chromatography. The preparation was formed a single band on SDS-PAGE. The purification multiple was 133.68, and the specific activity 2.5U/mg. The molecular weight of AMP deaminase was 178ku determined with gel filtration and its subunit weight was 87ku determined with SDS-PAGE. Isoelectric focusing study showed that pI values of the enzyme were 6.81. This enzyme catalysis AMPD optimal pH of ammonia reaction were 5.9, pH in the range of 5.2～6.4 stability. The optimum temperature was 37℃, higher than 42℃ was not stable. AMP deaminased from different sources were basically the same activator and inhibitor.