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Identifier uch.med.phd//1993kritis
Title Σχέση δομής-λειτουργίας της απολιποπρωτεΐνης Β του ανθρώπου
Alternative Title Structure-fuction relationship of human apolipoprotein B
Creator Kritis, Aristeidis
Abstract In the present study evidence is presented concerning the investigation of the intracellular mecahnism with which apoB assembles with lipids to form lipoprotein and clarification of the role of secondary and tertiary structure of the protein and possibly of enzymatic activities in the formation of LDL. Two complementary experimental approaches were followed. The first dealt with expressing and analyzing hybrid proteins consisting of almost all of apoAI protein and consecutive overlapping fragments of apoB inserted at the corboxyl terminal end of apoAI between the residues 212-233, and analysis of the resulting proteins for their ability to form lipoprotein. The second approach dealt with expressing aminoterminal fragemnts of apoB (B29, B43 and B47) and analyzing them for their ability to form lipoprotein. The experimental data lead us to conclude that the ability of apoB48 for intracellullar assembly into lipoprotein is not due to specific sequences present on dinstict fragments of apoB48 and that the length of apoB required for lipoptotein formation in C217 is more than 29% and equal or less that 41% of its molecule. Our conclusions are in agreement with a model in which apoB after its synthesis assumes the correct tertiary structure that allows (enzymatic or not) intracellular assemly with lipids. In addition lopoprotein formation in non hepatic C217 cells signifies that possible enzymatic activities or other protein required for lipoprotein assembly are not tissue specific.
Issue date 1993-01-01
Date available 1997-06-6
Collection   School/Department--School of Medicine--Department of Medicine--Doctoral theses
  Type of Work--Doctoral theses
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