Isolation and Partial Characterization of Lecithin Cholesterol Acyltransferase and High Density Lipoprotein from Hog Plasma

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Lecithin:cholesterol acyltransferase (LCAT) was purified 30,000-fold from hog plasma in a homogeneous state as indicated by polyacrylamide gel electrophoresis. The purified enzyme had an apparent molecular weight of 66,000 and was found to contain about 21.4 percent (w/w) carbohydrate. The properties of hog LCAT including amino acid composition were compared with human LCAT. High density lipoprotein (HDL) was isolated from the hog plasma by an immunoaffinity column chromatography. The isolated HDL showed nearly identical lipid-protein composition although it contained additional protein components when it was compared to HDL isolated by a traditional method involving ultracentrifugation.

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vi, 78 leaves: ill.

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Park, Yong Bok May 1984.

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  • Park, Yong Bok

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Lecithin:cholesterol acyltransferase (LCAT) was purified 30,000-fold from hog plasma in a homogeneous state as indicated by polyacrylamide gel electrophoresis. The purified enzyme had an apparent molecular weight of 66,000 and was found to contain about 21.4 percent (w/w) carbohydrate. The properties of hog LCAT including amino acid composition were compared with human LCAT. High density lipoprotein (HDL) was isolated from the hog plasma by an immunoaffinity column chromatography. The isolated HDL showed nearly identical lipid-protein composition although it contained additional protein components when it was compared to HDL isolated by a traditional method involving ultracentrifugation.

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vi, 78 leaves: ill.

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  • May 1984

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  • May 10, 2015, 6:16 a.m.

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Park, Yong Bok. Isolation and Partial Characterization of Lecithin Cholesterol Acyltransferase and High Density Lipoprotein from Hog Plasma, thesis, May 1984; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc504140/: accessed May 25, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .