The purification of acid phosphatase from honey bee venom (Apis mellifica)
Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weigh...
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| Veröffentlicht in: | Toxicon (Oxford) 1987, Vol.25 (10), p.1097-1103 |
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| container_end_page | 1103 |
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| container_issue | 10 |
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| container_title | Toxicon (Oxford) |
| container_volume | 25 |
| creator | Barboni, E. Kemeny, D.M. Campos, S. Vernon, C.A. |
| description | Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin. |
| doi_str_mv | 10.1016/0041-0101(87)90266-2 |
| format | Article |
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The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin.</description><identifier>ISSN: 0041-0101</identifier><identifier>EISSN: 1879-3150</identifier><identifier>DOI: 10.1016/0041-0101(87)90266-2</identifier><identifier>PMID: 3424390</identifier><identifier>CODEN: TOXIA6</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>acid phosphatase ; Acid Phosphatase - isolation & purification ; allergens ; Ammonium Sulfate ; Analytical, structural and metabolic biochemistry ; Animals ; Apis mellifera ; Bee Venoms - analysis ; Biological and medical sciences ; Chromatography, Gel ; Chromatography, Ion Exchange ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Hydrolases ; purification ; venoms</subject><ispartof>Toxicon (Oxford), 1987, Vol.25 (10), p.1097-1103</ispartof><rights>1987</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c410t-7a8086d006f26207e09f5d8830955c203d2b6f9ba38f5f1eee7cabe61c634c6a3</citedby><cites>FETCH-LOGICAL-c410t-7a8086d006f26207e09f5d8830955c203d2b6f9ba38f5f1eee7cabe61c634c6a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0041-0101(87)90266-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,4009,27902,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7571763$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3424390$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Barboni, E.</creatorcontrib><creatorcontrib>Kemeny, D.M.</creatorcontrib><creatorcontrib>Campos, S.</creatorcontrib><creatorcontrib>Vernon, C.A.</creatorcontrib><title>The purification of acid phosphatase from honey bee venom (Apis mellifica)</title><title>Toxicon (Oxford)</title><addtitle>Toxicon</addtitle><description>Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin.</description><subject>acid phosphatase</subject><subject>Acid Phosphatase - isolation & purification</subject><subject>allergens</subject><subject>Ammonium Sulfate</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Apis mellifera</subject><subject>Bee Venoms - analysis</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases</subject><subject>purification</subject><subject>venoms</subject><issn>0041-0101</issn><issn>1879-3150</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi0EKkvhH4DwAVXtITC2E39ckKoKWlAlDrRny3HGrNEmDna2Uv99vd3VHjnNjOZ5R6OHkPcMPjNg8gtAyxqo7blWFwa4lA1_QVZMK9MI1sFLsjoir8mbUv4CgNBGnpAT0fJWGFiRn3drpPM2xxC9W2KaaArU-TjQeZ3KvHaLK0hDTiNdpwkfaY9IH3Cq8_nlHAsdcbN5Dl-8Ja-C2xR8d6in5P77t7urm-b21_WPq8vbxrcMlkY5DVoOADJwyUEhmNANWgswXec5iIH3MpjeCR26wBBRedejZF6K1ksnTsnZ_u6c078tlsWOsfj6hpswbYtVynAwnFWw3YM-p1IyBjvnOLr8aBnYnUK782N3fqxW9lmh5TX24XB_2484HEMHZ3X_6bB3xbtNyG7ysRwx1SmmpKjYxz0WXLLuT67I_W8OTAAHKVmrK_F1T2C19RAx2-IjTh6HmNEvdkjx_58-AasUlHA</recordid><startdate>1987</startdate><enddate>1987</enddate><creator>Barboni, E.</creator><creator>Kemeny, D.M.</creator><creator>Campos, S.</creator><creator>Vernon, C.A.</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><scope>FBQ</scope><scope>IQODW</scope><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>7X8</scope></search><sort><creationdate>1987</creationdate><title>The purification of acid phosphatase from honey bee venom (Apis mellifica)</title><author>Barboni, E. ; Kemeny, D.M. ; Campos, S. ; Vernon, C.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c410t-7a8086d006f26207e09f5d8830955c203d2b6f9ba38f5f1eee7cabe61c634c6a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>acid phosphatase</topic><topic>Acid Phosphatase - isolation & purification</topic><topic>allergens</topic><topic>Ammonium Sulfate</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Apis mellifera</topic><topic>Bee Venoms - analysis</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolases</topic><topic>purification</topic><topic>venoms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barboni, E.</creatorcontrib><creatorcontrib>Kemeny, D.M.</creatorcontrib><creatorcontrib>Campos, S.</creatorcontrib><creatorcontrib>Vernon, C.A.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Toxicon (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barboni, E.</au><au>Kemeny, D.M.</au><au>Campos, S.</au><au>Vernon, C.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The purification of acid phosphatase from honey bee venom (Apis mellifica)</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>1987</date><risdate>1987</risdate><volume>25</volume><issue>10</issue><spage>1097</spage><epage>1103</epage><pages>1097-1103</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><coden>TOXIA6</coden><abstract>Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>3424390</pmid><doi>10.1016/0041-0101(87)90266-2</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0041-0101 |
| ispartof | Toxicon (Oxford), 1987, Vol.25 (10), p.1097-1103 |
| issn | 0041-0101 1879-3150 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | acid phosphatase Acid Phosphatase - isolation & purification allergens Ammonium Sulfate Analytical, structural and metabolic biochemistry Animals Apis mellifera Bee Venoms - analysis Biological and medical sciences Chromatography, Gel Chromatography, Ion Exchange Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases purification venoms |
| title | The purification of acid phosphatase from honey bee venom (Apis mellifica) |
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