2026-09-22T00:56:46Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/84877 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Embargo set by: Seth Robbins for item 86158 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs The mechanism of membrane domain formation was investigated through analysis of domains induced both by calcium and myelin basic protein in vesicles containing components normally enriched in myelin. In the presence of calcium or myelin basic protein, domains enriched in phosphatidic acid, phosphatidylserine, galactocerebroside, and sulfatide were observed to form. In these domains phosphatidic acid or phosphatidylserine co-localized with galactocerebroside and sulfatide. Sphingomyelin was unable to partition into a domain unless sulfatide was also present. U of I Only Glaser, Michael Harvey, John Jay 2015-09-25T22:28:18Z 2015-09-25T22:28:18Z 10000-01-01 1997 1997 Made available in DSpace on 2015-09-25T22:28:18Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9717283.pdf: 6031051 bytes, checksum: 6a69c946880dc480dc03dd35314c672c (MD5) Previous issue date: 1997 Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs 214 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997. http://hdl.handle.net/2142/84877 (MiAaPQ)AAI9717283 eng Biology, Molecular Use of Fluorescence to Study the Membrane Binding Domain of Cytochrome B(5) and the Induction of Membrane Domain Formation in Phospholipid Vesicles by Myelin Basic Protein text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.