CATALYTIC PROPERTIES AND STABILITY OF LIPASE PURIFIED FROM HUMAN PANCREATIC-JUICE

Catalytic properties of a preparation of human pancreatic lipase purif ied from pancreatic juice have been compared to those of the enzyme pr esent in pooled plasma from patients suffering from acute pancreatitis . They were very similar as regards influence of effecters (sodium deo xycholate, colipase and Ca2+), optimal pH and apparent K-M in optimize d conditions. The stability of the preparation appeared to be satisfac tory. It was found to be stable for at least 200 days in a liquid form at +4 degrees C and predictive degradation rates per year of the lyop hilized form at +4 degrees C and -20 degrees C were 0.06% and 0.00%, r espectively. The close similarity of properties of this preparation wi th those of a recombinant human pancreatic lipase produced in V79 Chin ese hamster lung cells suggests that both approaches (purification fro m human pancreatic juice and gene transfer technology) could be used t o produce a suitable reference material for this enzyme.