Isolation, Physical and Chemical Characterization of Lecithin:Cholesterol Acyltransferase from Human Plasma

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The physiological role of LCAT has been the subject of a number of recent articles (Glomset, 1979; Nilsson-Ehle et al., 1980). According to most current theories, the enzyme functions in combination with high-density lipoproteins in the reverse cholesterol transport pathway which presumably returns peripheral cholesterol to the liver where cholesterol catabolism takes place. Despite the exciting potential for studies on the catalytic function and the nature of the enzyme-substrate complex, the mechanism of action of LCAT remains largely unexplored. The relatively slow progress in the elucidation of the LCAT reaction mechanism is likely to be due to the difficulties in ... continued below

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vi, 95 leaves : ill.

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Chong, Kui Song December 1981.

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  • Chong, Kui Song

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The physiological role of LCAT has been the subject of a number of recent articles (Glomset, 1979; Nilsson-Ehle et al., 1980). According to most current theories, the enzyme functions in combination with high-density lipoproteins in the reverse cholesterol transport pathway which presumably returns peripheral cholesterol to the liver where cholesterol catabolism takes place. Despite the exciting potential for studies on the catalytic function and the nature of the enzyme-substrate complex, the mechanism of action of LCAT remains largely unexplored. The relatively slow progress in the elucidation of the LCAT reaction mechanism is likely to be due to the difficulties in the isolation of the enzyme in sufficient quantities. Consequently, considerably less is known about the physical and chemical properties of the enzyme. Therefore, the first objective of this investigation was to isolate and purify sufficient amount of enzyme for subsequent characterization studies. The second objective of this investigation was to characterize the physical properties of the enzyme by techniques including analytical ultracentrifugation, ultraviolet spectroscopy, and circular dichroism and fluorescence spectroscopy. The third objective of this investigation was to characterize the chemical properties of the enzyme which deals with the amino acid and carbohydrate composition and with some basic structural features that are related to the chemical composition of LCAT.

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vi, 95 leaves : ill.

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UNT Theses and Dissertations

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  • December 1981

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  • Aug. 22, 2014, 6 p.m.

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  • June 12, 2018, 1:40 p.m.

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Chong, Kui Song. Isolation, Physical and Chemical Characterization of Lecithin:Cholesterol Acyltransferase from Human Plasma, dissertation, December 1981; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc331719/: accessed July 19, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .