Some physicochemical properties of human milk bile-salt activated lipase.
Influence of pH, deoxycholate and denaturing reagents on human milk bile-salt activated lipase (EC 3.1.1.3) has been studied. It appears that pH between 5.0-8.0 has no significant effect on the secondary structure of this lipase, but its higher order structures are affected. Lipase-dependent 8-anilino-1-naphthalene sulphonate fluorescence has revealed that the deoxycholate activated form of lipase has a surface rich in hydrophobic amino acid residues. Circular dichroism and second derivative electronic absorption spectroscopic observations have also provided an evidence for deoxycholate-induced alterations in the surface conformation of this lipase.
Singh
S
S
Division of Biopolymers Central Drug Research Institute, Lucknow.
Gupta
J
J
D001647:Bile Acids and Salts / Q000494:pharmacology; D002942:Circular Dichroism; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008895:Milk, Human / Q000201:enzymology*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
D001647:Bile Acids and Salts; D008049:Lipase