<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-22T23:52:12Z</responseDate><request verb="GetRecord" identifier="oai:digital.library.adelaide.edu.au:2440/19259" metadataPrefix="dim">https://digital.library.adelaide.edu.au/server/oai/request</request><GetRecord><record><header><identifier>oai:digital.library.adelaide.edu.au:2440/19259</identifier><datestamp>2015-09-22T04:16:35Z</datestamp><setSpec>com_2440_14759</setSpec><setSpec>col_2440_14760</setSpec></header><metadata><dim:dim xmlns:dim="http://www.dspace.org/xmlns/dspace/dim" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.dspace.org/xmlns/dspace/dim http://www.dspace.org/schema/dim.xsd">
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en">Kotlarski, Nicholas</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="school" lang="en">Dept. of Chemical Engineering</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en">1998</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">http://hdl.handle.net/2440/19259</dim:field>
   <dim:field mdschema="dc" element="description" lang="en">Bibliography: leaves 215-236.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en">x, 249 leaves : ill. ; 30 cm.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en">Scale-up of a biochemical process involving expression of an Insulin-like Growth Factor-I analogue (LongR3IGF-I) as inclusion bodies within the bacterium Escherichia coli has been investigated. The principal focus was directed to the operation of refolding wherein the biological potency of the protein is imparted.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="dissertation" lang="en">Thesis (Ph.D.)--University of Adelaide, Dept. of Chemical Engineering, 1998?</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en">211980 bytes</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="mimetype" lang="en">application/pdf</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en">en</dim:field>
   <dim:field mdschema="dc" element="subject" qualifier="ddc" lang="en">660.63 21</dim:field>
   <dim:field mdschema="dc" element="subject" qualifier="lcsh" lang="en">Recombinant proteins Analysis.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en">Process-scale renaturation of recombinant proteins from inclusion bodies / by Nicholas Kotlarski.</dim:field>
   <dim:field mdschema="dc" element="type" lang="en">Thesis</dim:field>
   <dim:field mdschema="dc" element="provenance" lang="en">This electronic version is made publicly available by the University of Adelaide in accordance with its open access policy for student theses. Copyright in this thesis remains with the author. This thesis may incorporate third party material which has been used by the author pursuant to Fair Dealing exception. If you are the author of this thesis and do not wish it to be made publicly available or If you are the owner of any included third party copyright material you wish to be removed from this electronic version, please complete the take down form located at: http://www.adelaide.edu.au/legals.</dim:field>open.access</dim:dim></metadata></record></GetRecord></OAI-PMH>