Partial purification of locust flight muscle lipoprotein lipase (LpL): apparent differences from mammalian LpL.
1. An attempt was made to purify lipoprotein lipase (LpL) from the flight muscle of the migratory locust based on affinity for heparin, which is known to avidly bind mammalian LpL. 2. However, locust LpL appeared to completely lack this property, which indicates that the suggested membrane-binding of locust LpL is very different from that of mammalian LpL: a heparin-like glycosaminoglycan is not involved. 3. Since locust LpL lacks heparin affinity, other purification methods were assayed. Solubilization of locust LpL was obtained by the detergent Tween 20. 4. Though both anion and cation exchange chromatography resulted in the complete loss of enzyme activity, partial purification of locust LpL was achieved by gel filtration chromatography.
Department of Experimental Zoology, University of Utrecht, The Netherlands.
M C
MC
van Heusden
D J
DJ
van der Horst
J M
JM
van Doorn
A M
AM
Beenakkers
D000818:Animals; D002846:Chromatography, Affinity; D005426:Flight, Animal; D006110:Grasshoppers / Q000201:enzymology*; D008071:Lipoprotein Lipase / Q000302:isolation & purification*; D008297:Male; D009132:Muscles / Q000201:enzymology*; D051381:Rats / Q000378:metabolism; D013045:Species Specificity; D013379:Substrate Specificity
D008071:Lipoprotein Lipase