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

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.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc331719
Date12 1900
CreatorsChong, Kui Song
ContributorsLacko, Andras G., Harris, Ben G., Gracy, Robert W., Jacobson, Myron, Norton, S. J.
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatvi, 95 leaves : ill., Text
RightsPublic, Chong, Kui Song, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved.

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