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Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from Celosia plumosa
Considering Celosia plumosa as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on Nicotiana glutinosa . By using 60% ammonium sulphate-precipitation, FPLC-based anion and ca...
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| Published in: | Physiology and molecular biology of plants 2019-01, Vol.25 (1), p.243-251 |
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| container_title | Physiology and molecular biology of plants |
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| creator | Gholizadeh, Ashraf |
| description | Considering
Celosia plumosa
as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on
Nicotiana glutinosa
. By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS–PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of
C
.
plumosa
at vegetative growth stage. The purified protein showed FRAP-based antioxidant activity in vitro and caused 1.7-fold and 1.4-fold increases in the growth rate of root system upon carborundum-based application on the root growth medium of
N
.
glutinosa
. The present work reports an antiviral protein with ribosome-inactivating, antioxidation and root developer potencies in
C. plumosa
as an edible or ornamental plant that may be useful in health and agricultural biotechnology in the future. |
| doi_str_mv | 10.1007/s12298-018-0577-5 |
| format | article |
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Celosia plumosa
as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on
Nicotiana glutinosa
. By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS–PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of
C
.
plumosa
at vegetative growth stage. The purified protein showed FRAP-based antioxidant activity in vitro and caused 1.7-fold and 1.4-fold increases in the growth rate of root system upon carborundum-based application on the root growth medium of
N
.
glutinosa
. The present work reports an antiviral protein with ribosome-inactivating, antioxidation and root developer potencies in
C. plumosa
as an edible or ornamental plant that may be useful in health and agricultural biotechnology in the future.</description><identifier>ISSN: 0971-5894</identifier><identifier>EISSN: 0974-0430</identifier><identifier>DOI: 10.1007/s12298-018-0577-5</identifier><identifier>PMID: 30804646</identifier><language>eng</language><publisher>New Delhi: Springer India</publisher><subject>Agricultural biotechnology ; Agricultural practices ; Ammonium ; Ammonium sulfate ; Anion exchanging ; Antioxidants ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biophysics ; Biotechnology ; Carborundum (trademark) ; Cation exchanging ; Cation-exchange chromatography ; Cell Biology ; Celosia ; Chromatography ; Gel electrophoresis ; Growth rate ; Growth stage ; Hypersensitive response ; Leaves ; Life Sciences ; Liquid chromatography ; Ornamental plants ; Plant Physiology ; Plant Sciences ; Protein folding ; Protein purification ; Proteins ; Research Article ; Ribosome-inactivating protein ; Size exclusion chromatography ; Sodium chloride ; Sodium lauryl sulfate ; Tobacco ; Viruses</subject><ispartof>Physiology and molecular biology of plants, 2019-01, Vol.25 (1), p.243-251</ispartof><rights>Prof. H.S. Srivastava Foundation for Science and Society 2018</rights><rights>Copyright Springer Nature B.V. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-c89a14c7cffe015568f30c8bee3b4348f914edded7a365a719e306c87d0a7ae3</citedby><cites>FETCH-LOGICAL-c470t-c89a14c7cffe015568f30c8bee3b4348f914edded7a365a719e306c87d0a7ae3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6352530/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6352530/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30804646$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gholizadeh, Ashraf</creatorcontrib><title>Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from Celosia plumosa</title><title>Physiology and molecular biology of plants</title><addtitle>Physiol Mol Biol Plants</addtitle><addtitle>Physiol Mol Biol Plants</addtitle><description>Considering
Celosia plumosa
as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on
Nicotiana glutinosa
. By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS–PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of
C
.
plumosa
at vegetative growth stage. The purified protein showed FRAP-based antioxidant activity in vitro and caused 1.7-fold and 1.4-fold increases in the growth rate of root system upon carborundum-based application on the root growth medium of
N
.
glutinosa
. The present work reports an antiviral protein with ribosome-inactivating, antioxidation and root developer potencies in
C. plumosa
as an edible or ornamental plant that may be useful in health and agricultural biotechnology in the future.</description><subject>Agricultural biotechnology</subject><subject>Agricultural practices</subject><subject>Ammonium</subject><subject>Ammonium sulfate</subject><subject>Anion exchanging</subject><subject>Antioxidants</subject><subject>Biological and Medical Physics</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Biotechnology</subject><subject>Carborundum (trademark)</subject><subject>Cation exchanging</subject><subject>Cation-exchange chromatography</subject><subject>Cell Biology</subject><subject>Celosia</subject><subject>Chromatography</subject><subject>Gel electrophoresis</subject><subject>Growth rate</subject><subject>Growth stage</subject><subject>Hypersensitive response</subject><subject>Leaves</subject><subject>Life Sciences</subject><subject>Liquid chromatography</subject><subject>Ornamental plants</subject><subject>Plant Physiology</subject><subject>Plant Sciences</subject><subject>Protein folding</subject><subject>Protein purification</subject><subject>Proteins</subject><subject>Research Article</subject><subject>Ribosome-inactivating protein</subject><subject>Size exclusion chromatography</subject><subject>Sodium chloride</subject><subject>Sodium lauryl sulfate</subject><subject>Tobacco</subject><subject>Viruses</subject><issn>0971-5894</issn><issn>0974-0430</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNp1kU2P1SAUhhujccbRH-DGkLhxUz0UKHRjYm78SibRxewJlx7uMGmhAr3qv5drx_EjcUEgvM95D4e3aZ5SeEkB5KtMu25QLdC6hJStuNecwyB5C5zB_Z9n2go18LPmUc43AD3jkj5szhgo4D3vz5vyeU3eeWuKj4FERwxJfh9znLH1wdjij1UKB7KkWNAH8tWXa2JCxb_5casyYSQpxkJGPOIUF0xkqXCwHjNxKc5kV6-zN2SZ1jlm87h54MyU8cntftFcvXt7tfvQXn56_3H35rK1XEJprRoM5VZa5xCoEL1yDKzaI7I9Z1y5gXIcRxylYb0wkg7IoLdKjmCkQXbRvN5sl3U_42gxlGQmvSQ_m_RdR-P130rw1_oQj7pnohMMqsGLW4MUv6yYi559tjhNJmBcs-6o6mn9x4FX9Pk_6E1cU6jTVUrWmEAxUSm6UTbFnBO6u8dQ0KdI9RaprpHqU6T6VPPszynuKn5lWIFuA3KVwgHT79b_d_0BqbGwFQ</recordid><startdate>20190101</startdate><enddate>20190101</enddate><creator>Gholizadeh, Ashraf</creator><general>Springer India</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20190101</creationdate><title>Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from Celosia plumosa</title><author>Gholizadeh, Ashraf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-c89a14c7cffe015568f30c8bee3b4348f914edded7a365a719e306c87d0a7ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Agricultural biotechnology</topic><topic>Agricultural practices</topic><topic>Ammonium</topic><topic>Ammonium sulfate</topic><topic>Anion exchanging</topic><topic>Antioxidants</topic><topic>Biological and Medical Physics</topic><topic>Biomedical and Life Sciences</topic><topic>Biophysics</topic><topic>Biotechnology</topic><topic>Carborundum (trademark)</topic><topic>Cation exchanging</topic><topic>Cation-exchange chromatography</topic><topic>Cell Biology</topic><topic>Celosia</topic><topic>Chromatography</topic><topic>Gel electrophoresis</topic><topic>Growth rate</topic><topic>Growth stage</topic><topic>Hypersensitive response</topic><topic>Leaves</topic><topic>Life Sciences</topic><topic>Liquid chromatography</topic><topic>Ornamental plants</topic><topic>Plant Physiology</topic><topic>Plant Sciences</topic><topic>Protein folding</topic><topic>Protein purification</topic><topic>Proteins</topic><topic>Research Article</topic><topic>Ribosome-inactivating protein</topic><topic>Size exclusion chromatography</topic><topic>Sodium chloride</topic><topic>Sodium lauryl sulfate</topic><topic>Tobacco</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gholizadeh, Ashraf</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Physiology and molecular biology of plants</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gholizadeh, Ashraf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from Celosia plumosa</atitle><jtitle>Physiology and molecular biology of plants</jtitle><stitle>Physiol Mol Biol Plants</stitle><addtitle>Physiol Mol Biol Plants</addtitle><date>2019-01-01</date><risdate>2019</risdate><volume>25</volume><issue>1</issue><spage>243</spage><epage>251</epage><pages>243-251</pages><issn>0971-5894</issn><eissn>0974-0430</eissn><abstract>Considering
Celosia plumosa
as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on
Nicotiana glutinosa
. By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS–PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of
C
.
plumosa
at vegetative growth stage. The purified protein showed FRAP-based antioxidant activity in vitro and caused 1.7-fold and 1.4-fold increases in the growth rate of root system upon carborundum-based application on the root growth medium of
N
.
glutinosa
. The present work reports an antiviral protein with ribosome-inactivating, antioxidation and root developer potencies in
C. plumosa
as an edible or ornamental plant that may be useful in health and agricultural biotechnology in the future.</abstract><cop>New Delhi</cop><pub>Springer India</pub><pmid>30804646</pmid><doi>10.1007/s12298-018-0577-5</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0971-5894 |
| ispartof | Physiology and molecular biology of plants, 2019-01, Vol.25 (1), p.243-251 |
| issn | 0971-5894 0974-0430 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6352530 |
| source | PubMed Central（OA）; Springer Link |
| subjects | Agricultural biotechnology Agricultural practices Ammonium Ammonium sulfate Anion exchanging Antioxidants Biological and Medical Physics Biomedical and Life Sciences Biophysics Biotechnology Carborundum (trademark) Cation exchanging Cation-exchange chromatography Cell Biology Celosia Chromatography Gel electrophoresis Growth rate Growth stage Hypersensitive response Leaves Life Sciences Liquid chromatography Ornamental plants Plant Physiology Plant Sciences Protein folding Protein purification Proteins Research Article Ribosome-inactivating protein Size exclusion chromatography Sodium chloride Sodium lauryl sulfate Tobacco Viruses |
| title | Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from Celosia plumosa |
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