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    <title>UTas ePrints - Positive and negative ion electrospray mass spectrometric studies of some amino acids and glutathione, and their interactions with alkali metal ions and methylmercury(II)</title>
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    <meta content="Canty, A.J." name="eprints.creators_name" />
<meta content="Colton, R." name="eprints.creators_name" />
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<meta content="Positive and negative ion electrospray mass spectrometric studies of some amino acids and glutathione, and their interactions with alkali metal ions and methylmercury(II)
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<meta content="Positive and negative ion electrospray mass spectrometry (ESMS) has been used to investigate solutions of some simple amino acids (glycine, histidine, methionine and cysteine) and the small peptide glutathione. Negative ion ESMS detected the simple anions [AA-H-] in each case (AA = amino acid) and often the dimeric species [(AA)2-H]- were also observed. In the positive ion mode ESMS allowed the observation of the protonated cluster ions [H(AA)x]+ (x = 1-4). Some interactions between alkali metal ions and the amino acids were observed, but in general the peaks in the ES mass spectra were weak and the alkali metal complexation could not compete with protonation. In contrast, methylmercury(II) reacted strongly with the amino acids and glutathione. In addition to species of 1:1 stoichiometry, all the amino acids gave peaks in their ES mass spectra corresponding to the ions [(MeHg)2(AA-H)]+, while glutathione gave a clear indication of the formation of a 3:l species." name="eprints.abstract" />
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<meta content="Positive and negative ion electrospray mass spectrometry (ESMS) has been used to investigate solutions of some simple amino acids (glycine, histidine, methionine and cysteine) and the small peptide glutathione. Negative ion ESMS detected the simple anions [AA-H-] in each case (AA = amino acid) and often the dimeric species [(AA)2-H]- were also observed. In the positive ion mode ESMS allowed the observation of the protonated cluster ions [H(AA)x]+ (x = 1-4). Some interactions between alkali metal ions and the amino acids were observed, but in general the peaks in the ES mass spectra were weak and the alkali metal complexation could not compete with protonation. In contrast, methylmercury(II) reacted strongly with the amino acids and glutathione. In addition to species of 1:1 stoichiometry, all the amino acids gave peaks in their ES mass spectra corresponding to the ions [(MeHg)2(AA-H)]+, while glutathione gave a clear indication of the formation of a 3:l species." name="DC.description" />
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    <h1 class="ep_tm_pagetitle">Positive and negative ion electrospray mass spectrometric studies of some amino acids and glutathione, and their interactions with alkali metal ions and methylmercury(II)</h1>
    <p style="margin-bottom: 1em" class="not_ep_block"><span class="person_name">Canty, A.J.</span> and <span class="person_name">Colton, R.</span> and <span class="person_name">D'Agostino, A.</span> and <span class="person_name">Traeger, J.C.</span> (1994) <xhtml:em>Positive and negative ion electrospray mass spectrometric studies of some amino acids and glutathione, and their interactions with alkali metal ions and methylmercury(II).</xhtml:em> Inorganica Chimica Acta, 223 (1 -2). pp. 103-107. ISSN 0020-1693</p><p style="margin-bottom: 1em" class="not_ep_block"></p><table style="margin-bottom: 1em" class="not_ep_block"><tr><td valign="top" style="text-align:center"><a href="http://eprints.utas.edu.au/2914/1/ICA1994_2C_103.pdf"><img alt="[img]" src="http://eprints.utas.edu.au/style/images/fileicons/application_pdf.png" class="ep_doc_icon" border="0" /></a></td><td valign="top"><a href="http://eprints.utas.edu.au/2914/1/ICA1994_2C_103.pdf"><span class="ep_document_citation">PDF</span></a> - Full text restricted - Requires a PDF viewer<br />494Kb</td><td><form method="get" accept-charset="utf-8" action="http://eprints.utas.edu.au/cgi/request_doc"><input accept-charset="utf-8" value="4281" name="docid" type="hidden" /><div class=""><input value="Request a copy" name="_action_null" class="ep_form_action_button" onclick="return EPJS_button_pushed( '_action_null' )" type="submit" /> </div></form></td></tr></table><p style="margin-bottom: 1em" class="not_ep_block">Official URL: <a href="http://dx.doi.org/10.1016/0020-1693(94)03999-2">http://dx.doi.org/10.1016/0020-1693(94)03999-2</a></p><div class="not_ep_block"><h2>Abstract</h2><p style="padding-bottom: 16px; text-align: left; margin: 1em auto 0em auto">Positive and negative ion electrospray mass spectrometry (ESMS) has been used to investigate solutions of some simple amino acids (glycine, histidine, methionine and cysteine) and the small peptide glutathione. Negative ion ESMS detected the simple anions [AA-H-] in each case (AA = amino acid) and often the dimeric species [(AA)2-H]- were also observed. In the positive ion mode ESMS allowed the observation of the protonated cluster ions [H(AA)x]+ (x = 1-4). Some interactions between alkali metal ions and the amino acids were observed, but in general the peaks in the ES mass spectra were weak and the alkali metal complexation could not compete with protonation. In contrast, methylmercury(II) reacted strongly with the amino acids and glutathione. In addition to species of 1:1 stoichiometry, all the amino acids gave peaks in their ES mass spectra corresponding to the ions [(MeHg)2(AA-H)]+, while glutathione gave a clear indication of the formation of a 3:l species.</p></div><table style="margin-bottom: 1em" cellpadding="3" class="not_ep_block" border="0"><tr><th valign="top" class="ep_row">Item Type:</th><td valign="top" class="ep_row">Article</td></tr><tr><th valign="top" class="ep_row">Additional Information:</th><td valign="top" class="ep_row">The definitive version is available at http://www.sciencedirect.com&#13;
</td></tr><tr><th valign="top" class="ep_row">Subjects:</th><td valign="top" class="ep_row"><a href="http://eprints.utas.edu.au/view/subjects/250204.html">250000 Chemical Sciences &gt; 250200 Inorganic Chemistry &gt; 250204 Bioinorganic Chemistry</a></td></tr><tr><th valign="top" class="ep_row">Collections:</th><td valign="top" class="ep_row">UNSPECIFIED</td></tr><tr><th valign="top" class="ep_row">ID Code:</th><td valign="top" class="ep_row">2914</td></tr><tr><th valign="top" class="ep_row">Deposited By:</th><td valign="top" class="ep_row"><span class="ep_name_citation"><span class="person_name">Prof Allan J Canty</span></span></td></tr><tr><th valign="top" class="ep_row">Deposited On:</th><td valign="top" class="ep_row">30 Jan 2008 14:16</td></tr><tr><th valign="top" class="ep_row">Last Modified:</th><td valign="top" class="ep_row">30 Jan 2008 14:16</td></tr><tr><th valign="top" class="ep_row">ePrint Statistics:</th><td valign="top" class="ep_row"><a target="ePrintStats" href="/es/index.php?action=show_detail_eprint;id=2914;">View statistics for this ePrint</a></td></tr></table><p align="right">Repository Staff Only: <a href="http://eprints.utas.edu.au/cgi/users/home?screen=EPrint::View&amp;eprintid=2914">item control page</a></p>
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