Lipases in bovine milk and the relationship between the lipoprotein lipase and tributyrate hydrolysing activities in cream and skim-milk.
The lipoprotein lipase and tributyrate hydrolysing activities were found to be similarly distributed in the fractions obtained when whole milk was separated into skim-milk and cream, and when the cream was washed and freed from lipid. These enzyme activities in skim-milks and in extracts of lipid-free cream could not be separated by affinity chromatography on heparin-Sepharose. The enzymes were inactivated to the same degree when incubated at 37 degrees C in the presence of 1-5 M-NaCl, pH 8-5,  and both showed marked decrease in stability at 4 degrees C in UV-light caused the same decrease in both lipoprotein lipase and tributyrate hydrolysing activities. An antiserum against a highly purified skim-milk lipoprotein lipase caused total inhibition of the lipoprotein lipase and tributyrate hydrolysing activities in skim-milk and in extracts of lipid-free cream. It is suggested that in bovine milk there is only one major lipase and that it is identical to lipoprotein lipase.
D000818:Animals; D002417:Cattle; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000378:metabolism / Q000528:radiation effects; D008055:Lipids / Q000032:analysis; D008071:Lipoprotein Lipase / Q000276:immunology / Q000378:metabolism* / Q000528:radiation effects; D008892:Milk / Q000032:analysis / Q000201:enzymology*; D011830:Radiation Effects; D012965:Sodium Chloride / Q000494:pharmacology; D014466:Ultraviolet Rays
D008055:Lipids; D012965:Sodium Chloride; D008049:Lipase; D008071:Lipoprotein Lipase