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First published online February 6, 2004
Journal of Experimental Biology 207, 897-903 (2004)
Published by The Company of Biologists 2004
doi: 10.1242/jeb.00823

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The substrate specificity of hormone-sensitive lipase from adipose tissue of the Antarctic fish Trematomus newnesi

J. R. Hazel¹ and B. D. Sidell^2,*

¹ Department of Biology, Arizona State University, Tempe, AZ 85287-1501, USA
² School of Marine Sciences, University of Maine, Orono, ME 04469-5751, USA

View larger version (19K): [in a new window]   Fig. 1. Elution profile of heparin–Sepharose affinity chromatography column illustrating the elution of protein (absorbance at 280 nm;solid symbols) and the concentration of NaCl in the eluate (open symbols). Typical results from a single experiment. Horizontal bars indicate those fractions with detectable lipase activity against TAG substrates. Activity eluting early in the column is HSL, which is not retarded by the heparin affinity column. Activity eluting later in the chromatogram at high salt concentration is LPL, which is retarded by the heparin affinity column.

View larger version (11K): [in a new window]   Fig. 2. The effects of various totally saturated species of triacylglycerol (TAG; e.g. T14:0 indicates the addition of trimyristoyl TAG) on rates of oleate release from triolein by hormone-sensitive lipase (HSL). Results are presented as means ± S.E.M. (N=4) for the ratio of the rate of oleate released in the presence of the substrate indicated on the abscissa compared with the rate measured with triolein. **P<0.0001; *0.0001<P<0.002, indicating significant differences compared with the addition of triolein.

View larger version (13K): [in a new window]   Fig. 3. The effects of various monoenoic species of triacylglycerol (TAG; e.g. T16:1 indicates the addition of tripalmitoleoyl TAG) on rates of oleate release from triolein by hormone-sensitive lipase (HSL). Results are presented as means ± S.E.M. (N=4) for the ratio of the rate of oleate released in the presence of the substrate indicated on the abscissa compared with the rate measured with triolein. *P<0.04, indicating significant differences compared with the addition of triolein.

View larger version (10K): [in a new window]   Fig. 4. The effects of polyenoic species of triacylglycerol (TAG; e.g. T20:4 indicates the addition of triarachidonyl TAG) on rates of oleate release from triolein by hormone-sensitive lipase (HSL). Results are presented as means ± S.E.M. (N=4) for the ratio of the rate of oleate released in the presence of the substrate indicated on the abscissa compared with the rate measured with triolein. *P<0.04, indicating significant differences compared with the addition of triolein.

View larger version (12K): [in a new window]   Fig. 5. The effects of differing positional isomers of diacylglycerol (DAG) species on rates of oleate release from triolein by hormone-sensitive lipase (HSL). Results are presented as means ± range (N=2) for the ratio of the rate of oleate released in the presence of the substrate indicated on the abscissa compared with the rate measured with triolein.