Effect of monoclonal anti-neuraminidase antibodies on the kinetic behaviour of influenza virus neuraminidase
Identifieur interne : 002672 ( Main/Exploration ); précédent : 002671; suivant : 002673Effect of monoclonal anti-neuraminidase antibodies on the kinetic behaviour of influenza virus neuraminidase
Auteurs : C. E. Mountford [Australie] ; G. Grossman [Australie] ; K. T. Holmes [Australie] ; W. J. O'Sullivan [Australie] ; A. W. Hampson [Australie] ; R. L. Raison [Australie] ; R. Webster [États-Unis]Source :
- Molecular Immunology [ 0161-5890 ] ; 1982.
English descriptors
- Teeft :
- Antigenic, Behaviour, Bucher kilbourne, Electron micrographs, Enzyme activity, Enzymic activity, High substrate concentrations, High substrate range, Immunizing virus, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Intact virus, Kendal eckert, Kinetic behaviour, Kinetics, Laver, Monoclonal, Monoclonal antibodies, Monoclonal neuraminidase antibodies, Multiphasic behaviour, Multiphasic plot, Nanlac, Neuraminidase, Neuraminidase activity, Neuraminidase heads, Pronase digestion, Rana, Recombinant, Substrate inhibition, Substrate nanlac, Uncomplexed enzyme, Viral neuraminidase, Virus, Virus complexed, Wana, Whole virus, Wide range.
Abstract
Abstract: Neuraminidase from the recombinant influenza virus A/NWSHA-Tokyo/3/67NA HON2 has been shown to exhibit non-Michaelis-Menten kinetics. The multiphasic behaviour was demonstrated for both the isolated neuraminidase heads and for the intact virus.Interaction of the enzyme with two monoclonal anti-neuraminidase antibodies (WANA 1 and RANA 1), which recognize separate antigenic determinants on the molecule, resulted in hyperbolic kinetic behaviour. While both antibodies abolished the multiphasic kinetics of the enzymic reaction, only WANA 1 altered the Vmax and Km values, indicating that it may in some way inhibit the interaction of enzyme and substrate.
Url:
DOI: 10.1016/0161-5890(82)90007-4
Affiliations:
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Box 138, Memphis, TN 38101</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Immunology</title><title level="j" type="abbrev">MIMM</title><idno type="ISSN">0161-5890</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1982">1982</date><biblScope unit="volume">19</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="811">811</biblScope><biblScope unit="page" to="816">816</biblScope></imprint><idno type="ISSN">0161-5890</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0161-5890</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Antigenic</term><term>Behaviour</term><term>Bucher kilbourne</term><term>Electron micrographs</term><term>Enzyme activity</term><term>Enzymic activity</term><term>High substrate concentrations</term><term>High substrate range</term><term>Immunizing virus</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Intact virus</term><term>Kendal eckert</term><term>Kinetic behaviour</term><term>Kinetics</term><term>Laver</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal neuraminidase antibodies</term><term>Multiphasic behaviour</term><term>Multiphasic plot</term><term>Nanlac</term><term>Neuraminidase</term><term>Neuraminidase activity</term><term>Neuraminidase heads</term><term>Pronase digestion</term><term>Rana</term><term>Recombinant</term><term>Substrate inhibition</term><term>Substrate nanlac</term><term>Uncomplexed enzyme</term><term>Viral neuraminidase</term><term>Virus</term><term>Virus complexed</term><term>Wana</term><term>Whole virus</term><term>Wide range</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Neuraminidase from the recombinant influenza virus A/NWSHA-Tokyo/3/67NA HON2 has been shown to exhibit non-Michaelis-Menten kinetics. The multiphasic behaviour was demonstrated for both the isolated neuraminidase heads and for the intact virus.Interaction of the enzyme with two monoclonal anti-neuraminidase antibodies (WANA 1 and RANA 1), which recognize separate antigenic determinants on the molecule, resulted in hyperbolic kinetic behaviour. While both antibodies abolished the multiphasic kinetics of the enzymic reaction, only WANA 1 altered the Vmax and Km values, indicating that it may in some way inhibit the interaction of enzyme and substrate.</div></front></TEI><affiliations><list><country><li>Australie</li><li>États-Unis</li></country><region><li>Nouvelle-Galles du Sud</li><li>Tennessee</li></region><settlement><li>Sydney</li></settlement><orgName><li>Université de Sydney</li></orgName></list><tree><country name="Australie"><noRegion><name sortKey="Mountford, C E" sort="Mountford, C E" uniqKey="Mountford C" first="C. E." last="Mountford">C. E. Mountford</name></noRegion><name sortKey="Grossman, G" sort="Grossman, G" uniqKey="Grossman G" first="G." last="Grossman">G. Grossman</name><name sortKey="Hampson, A W" sort="Hampson, A W" uniqKey="Hampson A" first="A. W." last="Hampson">A. W. Hampson</name><name sortKey="Holmes, K T" sort="Holmes, K T" uniqKey="Holmes K" first="K. T." last="Holmes">K. T. Holmes</name><name sortKey="O Sullivan, W J" sort="O Sullivan, W J" uniqKey="O Sullivan W" first="W. J." last="O'Sullivan">W. J. O'Sullivan</name><name sortKey="Raison, R L" sort="Raison, R L" uniqKey="Raison R" first="R. L." last="Raison">R. L. Raison</name></country><country name="États-Unis"><region name="Tennessee"><name sortKey="Webster, R" sort="Webster, R" uniqKey="Webster R" first="R." last="Webster">R. Webster</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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