Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom
We have investigated the effect of Vipera lebetina venom on capillary permeability and isolated an increasing capillary permeability protein (ICPP) which is devoid of arginine ester hydrolase and phospholipase A2 activities. This protein was purified with a yield of about 0.2% by fast protein liquid...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2000-02, Vol.268 (1), p.69-72 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Gasmi, Ammar Abidi, Ferid Srairi, Najet Oijatayer, Adel Karoui, Habib Elayeb, Mohamed |
| description | We have investigated the effect of Vipera lebetina venom on capillary permeability and isolated an increasing capillary permeability protein (ICPP) which is devoid of arginine ester hydrolase and phospholipase A2 activities. This protein was purified with a yield of about 0.2% by fast protein liquid chromatography (FPLC) using successively Superose 12, Mono Q, and Mono S columns and by high-pressure liquid chromatography (HPLC) on a C8 reverse-phase column. The purified protein migrated on SDS–PAGE as a band of about 27 kDa under nonreducing conditions and as a band of about 16 kDa under reducing conditions. Chromatography on a C8 column of reduced and alkylated protein yielded a single peak suggesting that this protein is homodimeric. This protein was refractory to Edman degradation chemistry. We used successfully a chemical unblocking involving the incubation of the protein with HCl in anhydrous methanol. The N-terminal amino acid sequence clearly shows considerable similarity to that of vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF). |
| doi_str_mv | 10.1006/bbrc.2000.2078 |
| format | Article |
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This protein was purified with a yield of about 0.2% by fast protein liquid chromatography (FPLC) using successively Superose 12, Mono Q, and Mono S columns and by high-pressure liquid chromatography (HPLC) on a C8 reverse-phase column. The purified protein migrated on SDS–PAGE as a band of about 27 kDa under nonreducing conditions and as a band of about 16 kDa under reducing conditions. Chromatography on a C8 column of reduced and alkylated protein yielded a single peak suggesting that this protein is homodimeric. This protein was refractory to Edman degradation chemistry. We used successfully a chemical unblocking involving the incubation of the protein with HCl in anhydrous methanol. The N-terminal amino acid sequence clearly shows considerable similarity to that of vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF).</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2000.2078</identifier><identifier>PMID: 10652214</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Biochemistry, Molecular Biology ; Capillary Permeability - drug effects ; Dimerization ; Endothelial Growth Factors - genetics ; Growth Substances - genetics ; Growth Substances - isolation & purification ; Growth Substances - pharmacology ; Life Sciences ; Lymphokines - genetics ; Mice ; Molecular Sequence Data ; Molecular Weight ; Platelet-Derived Growth Factor - genetics ; Protein Structure, Quaternary ; Sequence Homology, Amino Acid ; Toxicology ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors ; Viper Venoms - chemistry ; Viper Venoms - genetics ; Viper Venoms - toxicity ; Viperidae</subject><ispartof>Biochemical and biophysical research communications, 2000-02, Vol.268 (1), p.69-72</ispartof><rights>2000 Academic Press</rights><rights>Copyright 2000 Academic Press.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c444t-f9e8548009790307cfe416729e6820b0b7277d23060ad9ee988ba7be11569b1d3</citedby><cites>FETCH-LOGICAL-c444t-f9e8548009790307cfe416729e6820b0b7277d23060ad9ee988ba7be11569b1d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2000.2078$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10652214$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://riip.hal.science/pasteur-01984506$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Gasmi, Ammar</creatorcontrib><creatorcontrib>Abidi, Ferid</creatorcontrib><creatorcontrib>Srairi, Najet</creatorcontrib><creatorcontrib>Oijatayer, Adel</creatorcontrib><creatorcontrib>Karoui, Habib</creatorcontrib><creatorcontrib>Elayeb, Mohamed</creatorcontrib><title>Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>We have investigated the effect of Vipera lebetina venom on capillary permeability and isolated an increasing capillary permeability protein (ICPP) which is devoid of arginine ester hydrolase and phospholipase A2 activities. This protein was purified with a yield of about 0.2% by fast protein liquid chromatography (FPLC) using successively Superose 12, Mono Q, and Mono S columns and by high-pressure liquid chromatography (HPLC) on a C8 reverse-phase column. The purified protein migrated on SDS–PAGE as a band of about 27 kDa under nonreducing conditions and as a band of about 16 kDa under reducing conditions. Chromatography on a C8 column of reduced and alkylated protein yielded a single peak suggesting that this protein is homodimeric. This protein was refractory to Edman degradation chemistry. We used successfully a chemical unblocking involving the incubation of the protein with HCl in anhydrous methanol. The N-terminal amino acid sequence clearly shows considerable similarity to that of vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF).</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biochemistry, Molecular Biology</subject><subject>Capillary Permeability - drug effects</subject><subject>Dimerization</subject><subject>Endothelial Growth Factors - genetics</subject><subject>Growth Substances - genetics</subject><subject>Growth Substances - isolation & purification</subject><subject>Growth Substances - pharmacology</subject><subject>Life Sciences</subject><subject>Lymphokines - genetics</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Platelet-Derived Growth Factor - genetics</subject><subject>Protein Structure, Quaternary</subject><subject>Sequence Homology, Amino Acid</subject><subject>Toxicology</subject><subject>Vascular Endothelial Growth Factor A</subject><subject>Vascular Endothelial Growth Factors</subject><subject>Viper Venoms - chemistry</subject><subject>Viper Venoms - genetics</subject><subject>Viper Venoms - toxicity</subject><subject>Viperidae</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFu1DAQhi0EotvClSPyC2Q79nqd-Fit6LbSSu0BCjdr7EwUlySO7GxR4eXJKqjqhcuMNP7-0fhj7JOAtQDQl84lv5YAMJeyesNWAgwUUoB6y1bzWBfSiB9n7DznRwAhlDbv2ZkAvZVSqBX7c39MoQkepxAHjkPNdy0m9BOl8HsZxoYj36f4a2r59fwSU9GFn8S_t8G3_HbwiTBT5jscQ9dheub3lHpCF7owPfMmxZ4_hJES8o4cTWFA_kBD7D-wdw12mT7-6xfs2_WXr7ub4nC3v91dHQqvlJqKxlC1VRWAKQ1soPQNKaFLaUhXEhy4UpZlLTegAWtDZKrKYelIiK02TtSbC1Yse1vs7JhCP99oIwZ7c3WwI-aJjsmCMJXagn4SM79eeJ9izomal5AAe7JuT9btybo9WZ8Dn5fAeHQ91a_wRfMMVAtA8zefAiWbfaDBUx0S-cnWMfxv919LnZGK</recordid><startdate>20000205</startdate><enddate>20000205</enddate><creator>Gasmi, Ammar</creator><creator>Abidi, Ferid</creator><creator>Srairi, Najet</creator><creator>Oijatayer, Adel</creator><creator>Karoui, Habib</creator><creator>Elayeb, Mohamed</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope></search><sort><creationdate>20000205</creationdate><title>Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom</title><author>Gasmi, Ammar ; Abidi, Ferid ; Srairi, Najet ; Oijatayer, Adel ; Karoui, Habib ; Elayeb, Mohamed</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c444t-f9e8548009790307cfe416729e6820b0b7277d23060ad9ee988ba7be11569b1d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biochemistry, Molecular Biology</topic><topic>Capillary Permeability - drug effects</topic><topic>Dimerization</topic><topic>Endothelial Growth Factors - genetics</topic><topic>Growth Substances - genetics</topic><topic>Growth Substances - isolation & purification</topic><topic>Growth Substances - pharmacology</topic><topic>Life Sciences</topic><topic>Lymphokines - genetics</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Platelet-Derived Growth Factor - genetics</topic><topic>Protein Structure, Quaternary</topic><topic>Sequence Homology, Amino Acid</topic><topic>Toxicology</topic><topic>Vascular Endothelial Growth Factor A</topic><topic>Vascular Endothelial Growth Factors</topic><topic>Viper Venoms - chemistry</topic><topic>Viper Venoms - genetics</topic><topic>Viper Venoms - toxicity</topic><topic>Viperidae</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gasmi, Ammar</creatorcontrib><creatorcontrib>Abidi, Ferid</creatorcontrib><creatorcontrib>Srairi, Najet</creatorcontrib><creatorcontrib>Oijatayer, Adel</creatorcontrib><creatorcontrib>Karoui, Habib</creatorcontrib><creatorcontrib>Elayeb, Mohamed</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gasmi, Ammar</au><au>Abidi, Ferid</au><au>Srairi, Najet</au><au>Oijatayer, Adel</au><au>Karoui, Habib</au><au>Elayeb, Mohamed</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2000-02-05</date><risdate>2000</risdate><volume>268</volume><issue>1</issue><spage>69</spage><epage>72</epage><pages>69-72</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>We have investigated the effect of Vipera lebetina venom on capillary permeability and isolated an increasing capillary permeability protein (ICPP) which is devoid of arginine ester hydrolase and phospholipase A2 activities. This protein was purified with a yield of about 0.2% by fast protein liquid chromatography (FPLC) using successively Superose 12, Mono Q, and Mono S columns and by high-pressure liquid chromatography (HPLC) on a C8 reverse-phase column. The purified protein migrated on SDS–PAGE as a band of about 27 kDa under nonreducing conditions and as a band of about 16 kDa under reducing conditions. Chromatography on a C8 column of reduced and alkylated protein yielded a single peak suggesting that this protein is homodimeric. This protein was refractory to Edman degradation chemistry. We used successfully a chemical unblocking involving the incubation of the protein with HCl in anhydrous methanol. 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| subjects | Amino Acid Sequence Animals Biochemistry, Molecular Biology Capillary Permeability - drug effects Dimerization Endothelial Growth Factors - genetics Growth Substances - genetics Growth Substances - isolation & purification Growth Substances - pharmacology Life Sciences Lymphokines - genetics Mice Molecular Sequence Data Molecular Weight Platelet-Derived Growth Factor - genetics Protein Structure, Quaternary Sequence Homology, Amino Acid Toxicology Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factors Viper Venoms - chemistry Viper Venoms - genetics Viper Venoms - toxicity Viperidae |
| title | Purification and Characterization of a Growth Factor-like Which Increases Capillary Permeability from Vipera lebetina Venom |
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