Structural and functional studies of the C-terminal domain of human apolipoprotein A-I: Limited proteolysis and deletion mutagenesis

Limited proteolysis was used to study the domain structure and to produce a large N-terminal fragment of human apolipoprotein A-I (apoA-I). Digestion of reconstituted high density lipoprotein (rHDL) prepared with apoA-I and dipalmitoyl phosphatidylcholine (DPPC) or palmitoyloleoyl PC (POPC) by chymotrypsin, trypsin, elastase, or subtilisin generated a major fragment of $\sim$22 kDa. Under milder conditions proteolysis of lipid-free apoA-I produced a fragment of similar size. The fragments shared the same N-terminus as intact apoA-I and the chymotryptic fragment had a molecular weight of 22,384 as determined by mass spectrometry. Thus the fragment consists of the N-terminal 192 residues of apoA-I.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Ji, Yong

Contributors dc:contributor

• Jonas, Ana

• Biology, Molecular
• Chemistry, Biochemistry
• Health Sciences, General

Statement dc:rights

• Copyright 1996 Ji, Yong

Language dc:language

eng

Identifier

9780591087949
AAI9702551
(UMI)AAI9702551

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/22853