On the formation of a ternary complex between lipase, colipase and micelles of amphipathic compounds.
Pancreatic lipase, colipase and 1-glyceryl octyl ether or lysolecithin micelles were shown to form a ternary complex probably resulting from the fixation of the enzyme to the binary colipase-micelle association already well documented in the case of bile salt micelles. Kinetic assays show that the colipase favours the lipase activity on tributyrin emulsions in presence of 1-glyceryl octyl ether. The UV spectrum of a derivative of lipase in which two 2-hydroxy 5-nitrobenzyl groups are attached to tryptophan, is distinctly modified by addition of 1-glyceryl octyl ether micelles in the presence of colipase.
D015077:2-Hydroxy-5-nitrobenzyl Bromide; D000818:Animals; D003089:Colipases / Q000378:metabolism*; D003102:Colloids / Q000378:metabolism*; D004987:Ethers; D005990:Glycerol; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008244:Lysophosphatidylcholines / Q000378:metabolism; D008823:Micelles / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology; D011506:Proteins / Q000378:metabolism*; D013552:Swine
D003089:Colipases; D003102:Colloids; D004987:Ethers; D008244:Lysophosphatidylcholines; D008823:Micelles; D011506:Proteins; D015077:2-Hydroxy-5-nitrobenzyl Bromide; D008049:Lipase; D005990:Glycerol