[HTML][HTML] Binding of hepatic lipase to heparin: identification of specific heparin-binding residues in two distinct positive charge clusters
RA Sendak, DE Berryman, G Gellman, K Melford… - Journal of Lipid …, 2000 - ASBMB
The interaction of hepatic lipase (HL) with heparan sulfate is critical to the function of this
enzyme. The primary amino acid sequence of HL was compared to that of lipoprotein lipase
(LPL), a related enzyme that possesses several putative heparin-binding domains. Of the
three putative heparin-binding clusters of LPL (J. Biol. Chem. 1994. 269: 4626–4633; J.
Lipid Res. 1998. 39: 1310–1315), one was conserved in HL (Cluster 1; residues Lys 297–
Arg 300 in rat HL) and two were partially conserved (Cluster 2; residues Asp 307–Phe 320 …
enzyme. The primary amino acid sequence of HL was compared to that of lipoprotein lipase
(LPL), a related enzyme that possesses several putative heparin-binding domains. Of the
three putative heparin-binding clusters of LPL (J. Biol. Chem. 1994. 269: 4626–4633; J.
Lipid Res. 1998. 39: 1310–1315), one was conserved in HL (Cluster 1; residues Lys 297–
Arg 300 in rat HL) and two were partially conserved (Cluster 2; residues Asp 307–Phe 320 …