1187 NEUTRAL LIPASE (NL) ACTIVITY IN BOVINE AND HUMAN ADIPOSE TISSUE (AT)

Abstract

Using ¹⁴C triolein as substrate, the activity of NL in bovine and human AT was determined in a) the crude extract in PBS pH 7.4, b) the 105,000 xg supernatant (^S105 fx)> c) the pH 5.2 acetic acid precipitate redissolved in tris-Hcl pH 7.4 (pH 5.2 ppt), d) the pH 5.2 ppt solubilized in 3mM Nonadet P40 (sol. pH 5.2 ppt) and e) the aqueous fraction of the pH 5.2 ppt (Aq. Fx.). The results shown indicate that most of the original activity was recoverable in the ^S105 Fx. It also shows; that in contrast to published rat results, NL is several times more active in rat than in either bovine or human AT. Further while, in rat, there was a 35-fold purification achieved at the pH 5.2 ppt stage, there was only a 2-fold purification in the bovine and a 4-fold purification in the human AT at that stage. Solubilization with Nonadet P-40 appears to render both enzymes less measurable by the assay method employed. These data suggest that NL in human and bovine AT are more alike and differ in some important respects from NL in rat AT.

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