The pigeon pancreatic lipase

Abstract

Certain biochemical properties of lipase in aqueous extracts of an ether defatted dry powder of the pigeon pancresd were studied in a manometric system using tributyrin as substrate. No cation requirement for the enzymic activity could be demonstrated. This enzyme is activated by sodium taurocholate and is inhibited by Kerbs cycle intermediates and lactic acid. This lipase is activated about 600% by mercuric chloride at very low concentrations of the salt and inhibited by PCMB and HgCl/Sub/2 at higher concentrations. The enzyme solution does not seem to contain- SH or even sulphur in its protein and still behaves as if it is a sulphydryl enzyme in the presence of sulphydryl reagents. The enzyme appears to be a metallo-protein requiring metal (probably iron) and reactive NH/Sub/2 groups for its activity.