Journal of Lipid Research, Vol 17, 248-256, Copyright © 1976 by Lipid Research, Inc.
Mechanism of salt-mediated inhibition of lipoprotein lipase
CJ Fielding and PE Fielding
The activity of lipoprotein lipase isolated from rat postheparin plasma has
been determined with synthetic lipids, in the presence and absence of
apoprotein of the natural substrate very low density lipoprotein, as a
function of medium ion-pair concentration of a number of different
inorganic salts. The several kinetic effects of lipoprotein protein on
lipase activity were specifically and quantitatively reversed in the
presence of molar sodium chloride or solutions of equivalent effective ion
concentrations of other salts. Salt-mediated inhibition was fully
reversible by silution and was independent of substrate concentration.
Inhibition was a function of the identity of the salt anion within a
Hofmeister (lyotropic) series: I- greater than SCN- greater than NO3-
greater than Cl- greater than F-, and, in these terms, was not
significantly different for a series of inorganic chlorides (Li+, Na+, K+,
Cs+). The effects of salts on the natural lipoprotein substrates,
chylomicrons, and very low density lipoproteins were similar to those
obtained with a synthetic lipid-protein substrate complex. These findings
are discussed in the light of recent ideas on the activation of lipoprotein
lipase.
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