Journal of Lipid Research, Vol 31, 793-799, Copyright © 1990 by Lipid Research, Inc.

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Lipid transfer particle in locust hemolymph: purification and characterization

Y Hirayama and H Chino
Institute of Low Temperature Science, Hokkaido University, Sapporo, Japan.

A lipid transfer particle (LTP) from the hemolymph of adult male locusts, Locusta migratoria, was isolated and purified. The locust LTP exhibited its capacity to catalyze the exchange of diacylglycerol between low density lipophorin (LDLp) and high density lipophorin (HDLp). Contrary to the LTP reported for the tobacco hornworm, M. sexta, the locust LTP appeared to lack the capacity to promote net transfer of diacylglycerol to form an intermediate density lipophorin, although it seems premature to conclude the complete lack of such a capacity in locust LTP. The original concentration of LTP in hemolymph is assumed to be extremely low compared to that of lipophorin; only a catalytic amount of LTP may be present in the hemolymph (e.g., only 160 micrograms of LTP was obtained from the original hemolymph containing 400 mg protein). The molecular weight of intact LTP was estimated to be about 600,000 and the LTP was comprised of three glycosylated apoproteins, apoLTP-I (mol wt 310K), apoLTP-II (mol wt 89K), and apoLTP- III (mol wt 68K). The locust LTP contained significant amounts of lipids; the total lipid content amounted to 14.4% and the lipids were comprised of 17% hydrocarbons, 44% diacylglycerol, 8% cholesterol, 13% free fatty acid, and 18% phospholipids. The above molecular properties of locust LTP are essentially similar to those reported for M. sexta LTP.
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