Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme

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Lecithin:cholesterol acyltransferase (LCAT) was isolated from hog plasma and basic physicochemical properties and functionally important regions were investigated. Approximately one milligram of the enzyme was purified to apparent homogeneity with approximately a 20,000-fold increase in specific activity. In the plasma, hog LCAT was found to associate with high-density lipoproteins (HDL) probably through hydrophobic interactions with apolipoprotein A-I. HDL was the preferred lipoprotein substrate of the enzyme as its macromolecular substrate. The enzyme was found to contain 4 free sulfhydryl groups; at least one of these appeared to be essential for catalytic activity. The enzyme had a tendency to aggregate at ... continued below

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viii, 124 leaves: ill.

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Park, Yong Bok May 1987.

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  • Park, Yong Bok

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Lecithin:cholesterol acyltransferase (LCAT) was isolated from hog plasma and basic physicochemical properties and functionally important regions were investigated. Approximately one milligram of the enzyme was purified to apparent homogeneity with approximately a 20,000-fold increase in specific activity. In the plasma, hog LCAT was found to associate with high-density lipoproteins (HDL) probably through hydrophobic interactions with apolipoprotein A-I. HDL was the preferred lipoprotein substrate of the enzyme as its macromolecular substrate. The enzyme was found to contain 4 free sulfhydryl groups; at least one of these appeared to be essential for catalytic activity. The enzyme had a tendency to aggregate at high concentrations. More than half of the tryptophan and none of the tyrosine residues of the enzyme were shown to be exposed to the aqueous environment based on fluorescence and absorbance studies, respectively.

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viii, 124 leaves: ill.

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  • May 1987

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  • Aug. 22, 2014, 6 p.m.

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  • March 16, 2016, 12:09 p.m.

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Park, Yong Bok. Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme, dissertation, May 1987; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc331699/: accessed April 25, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .