Actinchinin, a novel antifungal protein from the gold kiwi fruit.
Identifieur interne : 000443 ( Main/Corpus ); précédent : 000442; suivant : 000444Actinchinin, a novel antifungal protein from the gold kiwi fruit.
Auteurs : Lixin Xia ; T B NgSource :
- Peptides [ 0196-9781 ] ; 2004.
English descriptors
- KwdEn :
- Actinidia (chemistry), Animals (MeSH), Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antifungal Agents (pharmacology), Botrytis (drug effects), Chromatography, High Pressure Liquid (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Fruit (chemistry), Fusarium (drug effects), Hot Temperature (MeSH), Inhibitory Concentration 50 (MeSH), Mice (MeSH), Mice, Inbred C57BL (MeSH), Mitogens (chemistry), Mitogens (isolation & purification), Mitogens (pharmacology), Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (pharmacology).
- MESH :
- chemical , chemistry : Antifungal Agents, Mitogens, Plant Proteins.
- chemistry : Actinidia, Fruit.
- drug effects : Botrytis, Fusarium.
- chemical , isolation & purification : Antifungal Agents, Mitogens, Plant Proteins.
- chemical , pharmacology : Antifungal Agents, Mitogens, Plant Proteins.
- Animals, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Hot Temperature, Inhibitory Concentration 50, Mice, Mice, Inbred C57BL.
Abstract
An antifungal protein designated actinchinin, with an N-terminal sequence different from that of the thaumatin-like antifungal protein from green kiwi fruit, was isolated from the gold kiwi fruit. The antifungal protein, unlike its counterpart from green kiwi fruit, did not exert antifungal activity against Botrytis cinerea, but was active against Fusarium oxysporum which was unresponsive to thaumatin-like protein from green kiwi fruit. Actinchinin was isolated using a protocol that comprised ion exchange chromatography on CM-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and gel filtration by FPLC on Superdex 75. Actinchinin was adsorbed on CM-cellulose, Affi-gel blue gel and Mono S. It was devoid of mitogenic activity toward mouse splenocytes. In contrast to thaumatin-like protein from green kiwi fruit, actinchinin lacked HIV-1 reverse transcriptase inhibiting activity.
DOI: 10.1016/j.peptides.2004.05.002
PubMed: 15245867
Links to Exploration step
pubmed:15245867Le document en format XML
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The antifungal protein, unlike its counterpart from green kiwi fruit, did not exert antifungal activity against Botrytis cinerea, but was active against Fusarium oxysporum which was unresponsive to thaumatin-like protein from green kiwi fruit. Actinchinin was isolated using a protocol that comprised ion exchange chromatography on CM-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and gel filtration by FPLC on Superdex 75. Actinchinin was adsorbed on CM-cellulose, Affi-gel blue gel and Mono S. It was devoid of mitogenic activity toward mouse splenocytes. In contrast to thaumatin-like protein from green kiwi fruit, actinchinin lacked HIV-1 reverse transcriptase inhibiting activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15245867</PMID><DateCompleted><Year>2005</Year><Month>02</Month><Day>10</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0196-9781</ISSN><JournalIssue CitedMedium="Print"><Volume>25</Volume><Issue>7</Issue><PubDate><Year>2004</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Peptides</Title><ISOAbbreviation>Peptides</ISOAbbreviation></Journal><ArticleTitle>Actinchinin, a novel antifungal protein from the gold kiwi fruit.</ArticleTitle><Pagination><MedlinePgn>1093-8</MedlinePgn></Pagination><Abstract><AbstractText>An antifungal protein designated actinchinin, with an N-terminal sequence different from that of the thaumatin-like antifungal protein from green kiwi fruit, was isolated from the gold kiwi fruit. The antifungal protein, unlike its counterpart from green kiwi fruit, did not exert antifungal activity against Botrytis cinerea, but was active against Fusarium oxysporum which was unresponsive to thaumatin-like protein from green kiwi fruit. Actinchinin was isolated using a protocol that comprised ion exchange chromatography on CM-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and gel filtration by FPLC on Superdex 75. Actinchinin was adsorbed on CM-cellulose, Affi-gel blue gel and Mono S. It was devoid of mitogenic activity toward mouse splenocytes. In contrast to thaumatin-like protein from green kiwi fruit, actinchinin lacked HIV-1 reverse transcriptase inhibiting activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xia</LastName><ForeName>Lixin</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ng</LastName><ForeName>T B</ForeName><Initials>TB</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Peptides</MedlineTA><NlmUniqueID>8008690</NlmUniqueID><ISSNLinking>0196-9781</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008934">Mitogens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C496149">actinchinin protein, Actinidia chinensis</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D029042" MajorTopicYN="N">Actinidia</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020171" MajorTopicYN="N">Botrytis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005638" MajorTopicYN="N">Fruit</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005670" MajorTopicYN="N">Fusarium</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020128" MajorTopicYN="N">Inhibitory Concentration 50</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008934" MajorTopicYN="N">Mitogens</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>03</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2004</Year><Month>04</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2004</Year><Month>05</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>7</Month><Day>13</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>2</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>7</Month><Day>13</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15245867</ArticleId><ArticleId IdType="doi">10.1016/j.peptides.2004.05.002</ArticleId><ArticleId IdType="pii">S0196978104001998</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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