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

Thumbnail image of item number 1 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.
Thumbnail image of item number 2 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.
Thumbnail image of item number 3 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.
Thumbnail image of item number 4 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.
Showing 1-4 of 133 pages in this dissertation.

PDF Version Also Available for Download.

Description

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

Physical Description

viii, 124 leaves: ill.

Creation Information

Park, Yong Bok May 1987.

Context

This dissertation is part of the collection entitled: UNT Theses and Dissertations and was provided by the UNT Libraries to the UNT Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 207 times. More information about this dissertation can be viewed below.

Who

People and organizations associated with either the creation of this dissertation or its content.

Author

Chair

Committee Members

Publisher

Rights Holder

For guidance see Citations, Rights, Re-Use.

  • Park, Yong Bok

Provided By

UNT Libraries

The UNT Libraries serve the university and community by providing access to physical and online collections, fostering information literacy, supporting academic research, and much, much more.

About | Browse this Partner

Contact Us

Corrections Questions

What

Descriptive information to help identify this dissertation. Follow the links below to find similar items on the Digital Library.

Degree Information

Description

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.

Physical Description

viii, 124 leaves: ill.

Language

Item Type

Identifier

Unique identifying numbers for this dissertation in the Digital Library or other systems.

Collections

This dissertation is part of the following collection of related materials.

UNT Theses and Dissertations

Theses and dissertations represent a wealth of scholarly and artistic content created by masters and doctoral students in the degree-seeking process. Some ETDs in this collection are restricted to use by the UNT community.

About | Browse this Collection

What responsibilities do I have when using this dissertation?

Digital Files

When

Dates and time periods associated with this dissertation.

Creation Date

  • May 1987

Added to The UNT Digital Library

  • Aug. 22, 2014, 6 p.m.

Description Last Updated

  • March 16, 2016, 12:09 p.m.

Usage Statistics

When was this dissertation last used?

Yesterday: 0
Past 30 days: 0
Total Uses: 207
More Statistics

Interact With This Dissertation

Here are some suggestions for what to do next.

Start Reading

Thumbnail image of item number 1 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.
Thumbnail image of item number 2 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.
Thumbnail image of item number 3 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.
Thumbnail image of item number 4 in: 'Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme'.

PDF Version Also Available for Download.

Citations, Rights, Re-Use

International Image Interoperability Framework

IIF Logo

We support the IIIF Presentation API

Links for Robots

Helpful links in machine-readable formats.

Archival Resource Key (ARK)

International Image Interoperability Framework (IIIF)

Metadata Formats

Images

URLs

Stats

Park, Yong Bok. Studies on Hog Plasma Lecithin:cholesterol Acyltransferase: Isolation and Characterization of the Enzyme, dissertation, May 1987; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc331699/: accessed May 27, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .

Back to Top of Screen