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.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc331699 |
| Date | 05 1900 |
| Creators | Park, Yong Bok |
| Contributors | Lacko, Andras G., Gracy, Robert W., Masaracchia, Ruthann A., Jacobson, Myron, Harris, Ben G. |
| Publisher | North Texas State University |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | viii, 124 leaves: ill., Text |
| Rights | Public, Park, Yong Bok, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved. |
Page generated in 0.0019 seconds