Title page for ETD etd-05042006-164523


Type of Document Dissertation
Author Keon, Brigitte H.
URN etd-05042006-164523
Title Fatty acid synthase is a major polypeptide constituent of cytosolic lipoprotein and is associated with components of the milk lipid secretory pathway
Degree PhD
Department Biochemistry and Nutrition
Advisory Committee
Advisor Name Title
Keenan, Thomas W. Committee Chair
Akers, Robert Michael Committee Member
Bevan, David R. Committee Member
Kennelly, Peter J. Committee Member
Potts, Malcolm Committee Member
Keywords
  • Lipoproteins Synthesis
  • Lactation
Date of Defense 1993-05-15
Availability restricted
Abstract

Most of the lipid present in lactating mammary gland cytosol was associated with a high molecular weight aggregate isolated from cytosol by gel exclusion chromatography or by density gradient centrifugation. The major polypeptide constituent of this lipoprotein aggregate was the monomer of fatty acid synthase (FAS). The major milk lipid globule proteins, butyrophilin (8u) and xanthine oxidase (XO) , as well as the small GTP-binding protein ARF, also were present. This lipoprotein complex was abundant in cytosol from lactating but not from involuting mammary glands. HPTLC analysis of lipids extracted from the low density FAS (LDFAS) complex demonstrated the presence of the five major milk phospholipids as well as triacylglycerols, cholesterol, unesterified fatty acids, and diacylglycerols. 32P-labeled phospholipids present in cytosol could be transferred to microlipid droplets (MLD) and endoplasmic reticulum (ER), in vitro, and could be precipitated along with FAS, and other polypeptide constituents of the LDFAS complex. Complexed FAS could be separated from noncorrlplexed FAS by density gradient centrifugation, native PAGE, and gel exclusion chromatography. A large amount of phospholipid consistently was retained with the complexed form of FAS. These results suggest that FAS migrates to a low density fraction by virtue of its association to other proteins and lipids.

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