<?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>2026-09-20T11:20:51Z</responseDate><request verb="GetRecord" identifier="oai:digital.library.adelaide.edu.au:2440/127525" metadataPrefix="dim">https://digital.library.adelaide.edu.au/server/oai/request</request><GetRecord><record><header><identifier>oai:digital.library.adelaide.edu.au:2440/127525</identifier><datestamp>2026-06-12T07:42:58Z</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="advisor">Elliott, W.H.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author">Parslow, Graham Royston</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="school" lang="en">School of Biological Sciences</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued">1978</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">http://hdl.handle.net/2440/127525</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en">1. A Sample of rat liver mitochondrial ALV-Synthetase was purified to a specific activity of 4,684 units/ mg, the highest activity yet observed from a mammalian source. 2. The sequence of purification steps that permitted the isolation of the high specific activity enzyme noted above was developed during the work reported here. The sequence of procedures finally used to purify a mitochondrial extract included 0-50% ammonium sulphate precipitation, 5-20% (w/v) polyethylene glycol precipation, CM-sephadex chromatography, Sephadex G-100 filtration, and electrophoresis. 3. Attempts to duplicate previously reported purifications of ALV-Synthetase by use of affinity chromatography were unsuccessful. 4. Isoelectric focusing gave no clearly useful or preparative separations of ALV-Synthetase in pH gradients.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="dissertation" lang="en">Thesis (M.Sc.) -- University of Adelaide, Dept. of Biochemistry, 1979</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en">en</dim:field>
   <dim:field mdschema="dc" element="title" lang="en">Investigation of purification procedures to isolate rat mitochondrial ẟ - aminolaevulinic acid synthetase</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 exceptions. 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>