Abstract

The hypothesis tested in the epitope stability study is that apo B bound to a synthetic core of iodipamide ethyl ester (IDE) particles retain stability, as detected by immunoreactivity of apo B epitopes with two monoclonal antibodies. The mAB 3.01 binds to the carboxy terminal end of apo B-1 00. The mAB T4 binds to the T4 peptide fragment at the amino terminal end of both apo B-1 00 and apo B-48. Stability of LDL-coated IDE was evaluated over 40 days when stored at -20C, 4C and 25C. Stability of reconstituted lyophilized IDE was evaluated over 42 days, starting with particles that had been lyophilized for 14 days. For the nonlyophilized LDL-coated IDE, lower temperatures (-20C and 4C) appear to be more effective in slowing down degradation of apo B, as the epitope immunoreactivity detected by the mABs was greater for these temperatures than for 25C. Reconstituted lyophilized LDL-coated IDE particles are effective in stabilizing apo B antigenic sites for at least 28 days. Interpretation of the results of the study must include a consideration of the length of time LDL was stored at 4C before being bound to IDE particles (13 days) and the length of time the LDL-coated IDE was stored at 4C before lyophilization (14 days, or a total age of 27 days for LDL in vitro). This suggests that a future study of apo B epitope stability utilizing LDL-coated IDE should use fresher LDL (apo B) for coating IDE, followed by immediate lyophilization.

Library of Congress Subject Headings

Blood lipoproteins--Analysis; Esters--Analysis; Atherosclerosis--Etiology

Publication Date

1993

Document Type

Thesis

Department, Program, or Center

School of Chemistry and Materials Science (COS)

Advisor

Sparks, Janet

Comments

Note: imported from RIT’s Digital Media Library running on DSpace to RIT Scholar Works. Physical copy available through RIT's The Wallace Library at: QP99.3.L52 A523 1993

Campus

RIT – Main Campus

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