Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi
A hyaluronidase, named BmHYA1, was purified from the venom of Chinese red scorpion ( Buthus martensi), using successive chromatography. The homogeneity of BmHYA1 was confirmed by SDS-PAGE and MALDI-TOF mass spectrometry. The molecular mass of BmHYA1 was 48,696 Da determined by MALDI-TOF MS. The opti...
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| Veröffentlicht in: | Comparative biochemistry and physiology. Toxicology & pharmacology 2008-09, Vol.148 (3), p.250-257 |
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| creator | Feng, Luo Gao, Rong Gopalakrishnakone, Ponnampalam |
| description | A hyaluronidase, named BmHYA1, was purified from the venom of Chinese red scorpion (
Buthus martensi), using successive chromatography. The homogeneity of BmHYA1 was confirmed by SDS-PAGE and MALDI-TOF mass spectrometry. The molecular mass of BmHYA1 was 48,696 Da determined by MALDI-TOF MS. The optimal temperature and pH of BmHYA1 were 50 °C and pH 4.5, respectively. It could be inhibited by DTT, Cu
2+, Fe
3+ or heparin, but not Mg
2+, Ca
2+, reduced glutathione,
l-cysteine or EDTA. The sequence of thirty N-terminal amino acids of BmHYA1 was obtained by Edman degradation, as TSADF KVVWE VPSIM CSKKF KICVT DLLTS; but no similarity was found to other venom hyaluronidases. Further, BmHYA1 can hydrolyze hyaluronan into relatively smaller oligosaccharides and modulate the expression of CD44 variant in the breast cancer cell line MDA-MB-231. |
| doi_str_mv | 10.1016/j.cbpc.2008.06.003 |
| format | Article |
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Buthus martensi), using successive chromatography. The homogeneity of BmHYA1 was confirmed by SDS-PAGE and MALDI-TOF mass spectrometry. The molecular mass of BmHYA1 was 48,696 Da determined by MALDI-TOF MS. The optimal temperature and pH of BmHYA1 were 50 °C and pH 4.5, respectively. It could be inhibited by DTT, Cu
2+, Fe
3+ or heparin, but not Mg
2+, Ca
2+, reduced glutathione,
l-cysteine or EDTA. The sequence of thirty N-terminal amino acids of BmHYA1 was obtained by Edman degradation, as TSADF KVVWE VPSIM CSKKF KICVT DLLTS; but no similarity was found to other venom hyaluronidases. Further, BmHYA1 can hydrolyze hyaluronan into relatively smaller oligosaccharides and modulate the expression of CD44 variant in the breast cancer cell line MDA-MB-231.</description><identifier>ISSN: 1532-0456</identifier><identifier>EISSN: 1878-1659</identifier><identifier>DOI: 10.1016/j.cbpc.2008.06.003</identifier><identifier>PMID: 18611448</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Breast Neoplasms ; Buthus martensii ; CD44 ; Cell Line, Tumor ; Enzyme Stability ; Humans ; Hyaluronan Receptors - biosynthesis ; Hyaluronic Acid - metabolism ; Hyaluronidase ; Hyaluronoglucosaminidase - antagonists & inhibitors ; Hyaluronoglucosaminidase - isolation & purification ; Hyaluronoglucosaminidase - metabolism ; Hydrogen-Ion Concentration ; N-terminal sequence ; Purification ; Scorpion venom ; Scorpion Venoms - antagonists & inhibitors ; Scorpion Venoms - enzymology ; Scorpion Venoms - isolation & purification ; Scorpion Venoms - metabolism ; Scorpions ; Temperature</subject><ispartof>Comparative biochemistry and physiology. Toxicology & pharmacology, 2008-09, Vol.148 (3), p.250-257</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-fd49770ec837fd15898aa9d68553b159a2085bda36b7bad4de5383a1e411299d3</citedby><cites>FETCH-LOGICAL-c482t-fd49770ec837fd15898aa9d68553b159a2085bda36b7bad4de5383a1e411299d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cbpc.2008.06.003$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18611448$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Feng, Luo</creatorcontrib><creatorcontrib>Gao, Rong</creatorcontrib><creatorcontrib>Gopalakrishnakone, Ponnampalam</creatorcontrib><title>Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi</title><title>Comparative biochemistry and physiology. Toxicology & pharmacology</title><addtitle>Comp Biochem Physiol C Toxicol Pharmacol</addtitle><description>A hyaluronidase, named BmHYA1, was purified from the venom of Chinese red scorpion (
Buthus martensi), using successive chromatography. The homogeneity of BmHYA1 was confirmed by SDS-PAGE and MALDI-TOF mass spectrometry. The molecular mass of BmHYA1 was 48,696 Da determined by MALDI-TOF MS. The optimal temperature and pH of BmHYA1 were 50 °C and pH 4.5, respectively. It could be inhibited by DTT, Cu
2+, Fe
3+ or heparin, but not Mg
2+, Ca
2+, reduced glutathione,
l-cysteine or EDTA. The sequence of thirty N-terminal amino acids of BmHYA1 was obtained by Edman degradation, as TSADF KVVWE VPSIM CSKKF KICVT DLLTS; but no similarity was found to other venom hyaluronidases. Further, BmHYA1 can hydrolyze hyaluronan into relatively smaller oligosaccharides and modulate the expression of CD44 variant in the breast cancer cell line MDA-MB-231.</description><subject>Animals</subject><subject>Breast Neoplasms</subject><subject>Buthus martensii</subject><subject>CD44</subject><subject>Cell Line, Tumor</subject><subject>Enzyme Stability</subject><subject>Humans</subject><subject>Hyaluronan Receptors - biosynthesis</subject><subject>Hyaluronic Acid - metabolism</subject><subject>Hyaluronidase</subject><subject>Hyaluronoglucosaminidase - antagonists & inhibitors</subject><subject>Hyaluronoglucosaminidase - isolation & purification</subject><subject>Hyaluronoglucosaminidase - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>N-terminal sequence</subject><subject>Purification</subject><subject>Scorpion venom</subject><subject>Scorpion Venoms - antagonists & inhibitors</subject><subject>Scorpion Venoms - enzymology</subject><subject>Scorpion Venoms - isolation & purification</subject><subject>Scorpion Venoms - metabolism</subject><subject>Scorpions</subject><subject>Temperature</subject><issn>1532-0456</issn><issn>1878-1659</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2r1DAUhoMo3uvoH3AhXblrPaf5aApudPDjwgU3ug5pckozdJoxaS9cf70ZZsCdd5VD8rwvSR7G3iI0CKg-HBo3nFzTAugGVAPAn7Fb1J2uUcn-eZklb2sQUt2wVzkfAEAKVC_ZDWqFKIS-ZdNdjrNdQ1wqu_jKTTZZt1IKfy6bcaxsNT3aeUtxCd5mqsYUj9U6UfVAS5kKsZ_CQuUkka-yi-l0Tn7e1mnL1dGmlZYcXrMXo50zvbmuO_br65ef--_1_Y9vd_tP97UTul3r0Yu-64Cc5t3oUepeW9t7paXkA8retqDl4C1XQzdYLzxJrrlFEoht33u-Y-8vvacUf2-UV3MM2dE824Xilo3qBVeq654EWwTVYgdPgii0Rij327H2AroUc040mlMK5f2PBsGcjZmDORszZ2MGlCnGSujdtX0bjuT_Ra6KCvDxAlD5tYdAyWQXaHHkQyK3Gh_D__r_AgKxp-U</recordid><startdate>20080901</startdate><enddate>20080901</enddate><creator>Feng, Luo</creator><creator>Gao, Rong</creator><creator>Gopalakrishnakone, Ponnampalam</creator><general>Elsevier Inc</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>7ST</scope><scope>C1K</scope><scope>SOI</scope><scope>7SS</scope><scope>7X8</scope></search><sort><creationdate>20080901</creationdate><title>Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi</title><author>Feng, Luo ; Gao, Rong ; Gopalakrishnakone, Ponnampalam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-fd49770ec837fd15898aa9d68553b159a2085bda36b7bad4de5383a1e411299d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Breast Neoplasms</topic><topic>Buthus martensii</topic><topic>CD44</topic><topic>Cell Line, Tumor</topic><topic>Enzyme Stability</topic><topic>Humans</topic><topic>Hyaluronan Receptors - biosynthesis</topic><topic>Hyaluronic Acid - metabolism</topic><topic>Hyaluronidase</topic><topic>Hyaluronoglucosaminidase - antagonists & inhibitors</topic><topic>Hyaluronoglucosaminidase - isolation & purification</topic><topic>Hyaluronoglucosaminidase - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>N-terminal sequence</topic><topic>Purification</topic><topic>Scorpion venom</topic><topic>Scorpion Venoms - antagonists & inhibitors</topic><topic>Scorpion Venoms - enzymology</topic><topic>Scorpion Venoms - isolation & purification</topic><topic>Scorpion Venoms - metabolism</topic><topic>Scorpions</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feng, Luo</creatorcontrib><creatorcontrib>Gao, Rong</creatorcontrib><creatorcontrib>Gopalakrishnakone, Ponnampalam</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Environment Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Environment Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Comparative biochemistry and physiology. Toxicology & pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feng, Luo</au><au>Gao, Rong</au><au>Gopalakrishnakone, Ponnampalam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi</atitle><jtitle>Comparative biochemistry and physiology. Toxicology & pharmacology</jtitle><addtitle>Comp Biochem Physiol C Toxicol Pharmacol</addtitle><date>2008-09-01</date><risdate>2008</risdate><volume>148</volume><issue>3</issue><spage>250</spage><epage>257</epage><pages>250-257</pages><issn>1532-0456</issn><eissn>1878-1659</eissn><abstract>A hyaluronidase, named BmHYA1, was purified from the venom of Chinese red scorpion (
Buthus martensi), using successive chromatography. The homogeneity of BmHYA1 was confirmed by SDS-PAGE and MALDI-TOF mass spectrometry. The molecular mass of BmHYA1 was 48,696 Da determined by MALDI-TOF MS. The optimal temperature and pH of BmHYA1 were 50 °C and pH 4.5, respectively. It could be inhibited by DTT, Cu
2+, Fe
3+ or heparin, but not Mg
2+, Ca
2+, reduced glutathione,
l-cysteine or EDTA. The sequence of thirty N-terminal amino acids of BmHYA1 was obtained by Edman degradation, as TSADF KVVWE VPSIM CSKKF KICVT DLLTS; but no similarity was found to other venom hyaluronidases. Further, BmHYA1 can hydrolyze hyaluronan into relatively smaller oligosaccharides and modulate the expression of CD44 variant in the breast cancer cell line MDA-MB-231.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18611448</pmid><doi>10.1016/j.cbpc.2008.06.003</doi><tpages>8</tpages></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Animals Breast Neoplasms Buthus martensii CD44 Cell Line, Tumor Enzyme Stability Humans Hyaluronan Receptors - biosynthesis Hyaluronic Acid - metabolism Hyaluronidase Hyaluronoglucosaminidase - antagonists & inhibitors Hyaluronoglucosaminidase - isolation & purification Hyaluronoglucosaminidase - metabolism Hydrogen-Ion Concentration N-terminal sequence Purification Scorpion venom Scorpion Venoms - antagonists & inhibitors Scorpion Venoms - enzymology Scorpion Venoms - isolation & purification Scorpion Venoms - metabolism Scorpions Temperature |
| title | Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi |
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