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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Chymotryptic cleavage of lipoprotein lipase. Identification of cleavage sites and functional studies of the truncated molecule.

Treatment of bovine lipoprotein lipase ( LPL) with chymotrypsin results in cleavage between residues Phe390-Ser391 and between Trp392-Ser393, indicating that this region is exposed in the native conformation of LPL. Two main fragments are generated, one large including the amino-terminus (chymotrypsin-truncated LPL = c- LPL) and one small, carboxy-terminal fragment. The small fragment is not stable, but is further degraded by the protease. Isolated c- LPL has full catalytic activity against tributyryl glycerol (tributyrin) and p-nitrophenyl butyrate, while the activity against emulsions of long-chain triacylglycerols and against liposomes is reduced and the activity against milk fat globules and chylomicrons is lost. Several properties of c- LPL were investigated. It was found that c- LPL interacts with apolipoprotein CII (apo CII) as efficiently as intact LPL. The truncated enzyme bound to liposomes and to emulsions of long-chain triacylglycerols as well as the intact enzyme did. In contrast, c- LPL did not bind to milk fat globules or to chylomicrons. The activity of c- LPL was more sensitive to inhibition by other lipid-binding proteins, e.g. apolipoprotein CIII (apo CIII), than was the intact enzyme. The affinity for heparin was as high with c- LPL as with intact LPL. Like intact LPL, c- LPL is dimeric in its active form, as evidenced by sucrose density gradient centrifugation. It is concluded that the reduced catalytic and lipid-binding properties of c- LPL compared with intact LPL are related to the properties of the substrate interface. It is speculated that the carboxy-terminal part of LPL contains a secondary lipid-binding site, which is important for activity against chylomicrons and related substrates.[1]


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