Nondenaturing protein electrotransfer of the esterase activity of lipolytic preparations.
Lipolytic enzymes subjected to nondenaturing polyacrylamide gel electrophoresis were electrophoretically transferred under nondenaturing conditions onto a solid-state matrix. Electrotransfer permitted the visualization of hydrolytic activity to the long-chain water insoluble substrate alpha-naphthyl palmitate. Four commercial preparations: a lipase from Candida cylindracea, an esterase from porcine liver, a lipase from Pseudomonas sp., and a cholesterol esterase from Pseudomonas fluorescens were examined.
Brahimi-Horn
M C
MC
Division of Wool Technology, Melbourne Laboratory, Parkville, Australia.
Guglielmino
M L
ML
Gaal
A M
AM
Sparrow
L G
LG
D002175:Candida / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting / Q000379:methods*; D008049:Lipase / Q000378:metabolism*; D008066:Lipolysis; D008722:Methods; D010168:Palmitates / Q000032:analysis; D011489:Protein Denaturation; D011549:Pseudomonas / Q000201:enzymology; D002787:Sterol Esterase / Q000378:metabolism*
D010168:Palmitates; C018110:naphthyl palmitate; D002787:Sterol Esterase; D008049:Lipase