J. Biochem, 1982, Vol. 92, No. 3 865-870
© 1982 Japanese Biochemical Society
research-article |
Mechanism of Inhibition of Hepatic Triglyceride Lipase from Human Postheparin Plasma by Apolipoproteins A-I and A-II1
*Second Department of Internal Medicine, Osaka University Medical School Fukushima, Fukushima-ku, Osaka, Osaka 553
**Department of Etiology and Pathophysiology, Research Institute of the National Cardiovascular Center Suita, Osaka 565
The present data describe the mechanism of the inhibitory effects of human plasma apolipoproteins A-I and A-II on hydrolysis of triglyceride catalyzed by hepatic triglyceride lipase using a substrate of triolein particles stabilized with gum arabic in vitro. The experimental data could well be described by a model in which apolipoproteins bound to the surface of lipid substrate particles inhibited the enzyme reaction. The values of Km obtained were similar with or without inhibitors and the calculated saturation levels of apolipoprotein binding to the lipid were in good agreement with those obtained in independent binding experiments.
1This work was supported in part by Grant-in-Aid for the Intractable Diseases from the Ministry of Health and Welfare of Japan (1980-1981), by Grant-in-Aid for Scientific Research No. 448387 from the Ministry of Education, Science and Culture of Japan (1981), by Grant-in-Aid for Scientific Research No. 570809 from the Ministry of Education, Science and Culture of Japan (1981), and by the Research Fund of the Yamanouchi Foundation on Metabolic Disorders (1981).
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