Hydrolysis of primary and secondary esters of glycerol by pancreatic juice.
The relative rates of hydrolysis of the secondary ester in glycerol 1,3-benzylidene 2-oleate and in glycerol 1,3-dihexadecyl ether 2-oleate, and of the primary and secondary esters in triolein were determined. Both unaltered and selectively inactivated rat pancreatic juice were used as sources of enzyme. It was found that rat pancreatic juice contains an enzyme that can hydrolyze fatty acids esterified at the 2-position of a glyceride. This enzyme is not pancreatic lipase. It may be sterol ester hydrolase. Partial glycerides, as well as complete glycerides, can serve as substrates. Pancreatic lipase, if it can hydrolyze the 2-positioned fatty acids of a triglyceride, does so at a very slow rate.
D000818:Animals; D002247:Carbon Isotopes; D002845:Chromatography; D002852:Chromatography, Ion Exchange; D002855:Chromatography, Thin Layer; D005227:Fatty Acids / Q000378:metabolism; D005782:Gels; D005989:Glycerides / Q000378:metabolism*; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D009829:Oleic Acids / Q000378:metabolism; D010189:Pancreatic Juice / Q000378:metabolism*; D051381:Rats; D012822:Silicon Dioxide; D014304:Triolein / Q000378:metabolism
D002247:Carbon Isotopes; D005227:Fatty Acids; D005782:Gels; D005989:Glycerides; D009829:Oleic Acids; D014304:Triolein; D012822:Silicon Dioxide; D008049:Lipase