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Effect of colipase on adsorption and activity of rat pancreatic lipase on emulsified tributyrin in the presence of bile salt
Author(s) -
Vandermeers A.,
Vandermeers-Piret M.C.,
Rathé J.,
Christophe J.
Publication year - 1975
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(75)80779-4
Subject(s) - boulevard , tributyrin , medical school , lipase , chemistry , library science , medicine , biochemistry , engineering , enzyme , computer science , medical education , civil engineering
The present work was undertaken to examine rat pancreatic lipase activity in relation to its ability to be adsorbed on emulsified tributyrin. This study was conducted at a supramicellar concentration of sodium taurodeoxycholate, between pH 6.0 and 8.0, and at different colipase concentrations. A pH adsorption curve was differentiated from the pH activity curve of lipase. The authors concluded that the socalled acid shift of the optimal pH for lipase action described earlier is due to the low adsorption rate of lipase on its substrate at alkaline pH rather than to a change of the pH dependence of the V(max) and K(m) of the enzyme.SCOPUS: ar.jinfo:eu-repo/semantics/publishe