The Hag-protease-II is a fibrin(ogen)ase from Hippasa agelenoides spider venom gland extract: Purification, characterization and its role in hemostasis
The current study describes the biochemical, biophysical and pharmacological properties of Hag-protease-II from Hippasa agelenoides spider venom gland extract. The Hag-protease-II was purified to homogeneity using gel filtration and ion-exchange chromatography. The molecular mass was found to be 28....
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| Veröffentlicht in: | Toxicon (Oxford) 2011-02, Vol.57 (2), p.248-258 |
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| creator | Devaraja, S. Girish, K.S. Gowtham, Y.N.J. Kemparaju, K. |
| description | The current study describes the biochemical, biophysical and pharmacological properties of Hag-protease-II from Hippasa agelenoides spider venom gland extract. The Hag-protease-II was purified to homogeneity using gel filtration and ion-exchange chromatography. The molecular mass was found to be 28.749 kDa by MALDI-TOF mass spectrometry. PMSF abolished the activity while EDTA, EGTA, IAA and 1, 10-phenanthrolene did not. Hag-protease-II hydrolyzed casein, fibrinogen and fibrin, however it did not hydrolyze gelatin, fibronectin and collagen types- I and IV. It was non-lethal and devoid of hemorrhagic, myotoxic and edema forming activities. It dose dependently reduced re-calcification time of citrated human plasma. Strikingly; the Hag-protease-II coagulated the factor X deficient congenital human plasma. It hydrolyzed Bβ-chain but, did not degrade Aα- and γ-chains of fibrinogen while, it hydrolyzed α-polymer and α-chain but not the β-chain and γ–γ dimers of partially cross-linked fibrin clot. The Hag-protease-II induced aggregation of human platelets in PRP dose dependently, however it did not interfere in collagen induced aggregation of PRP and washed human platelets. |
| doi_str_mv | 10.1016/j.toxicon.2010.11.018 |
| format | Article |
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The Hag-protease-II was purified to homogeneity using gel filtration and ion-exchange chromatography. The molecular mass was found to be 28.749 kDa by MALDI-TOF mass spectrometry. PMSF abolished the activity while EDTA, EGTA, IAA and 1, 10-phenanthrolene did not. Hag-protease-II hydrolyzed casein, fibrinogen and fibrin, however it did not hydrolyze gelatin, fibronectin and collagen types- I and IV. It was non-lethal and devoid of hemorrhagic, myotoxic and edema forming activities. It dose dependently reduced re-calcification time of citrated human plasma. Strikingly; the Hag-protease-II coagulated the factor X deficient congenital human plasma. It hydrolyzed Bβ-chain but, did not degrade Aα- and γ-chains of fibrinogen while, it hydrolyzed α-polymer and α-chain but not the β-chain and γ–γ dimers of partially cross-linked fibrin clot. The Hag-protease-II induced aggregation of human platelets in PRP dose dependently, however it did not interfere in collagen induced aggregation of PRP and washed human platelets.</description><identifier>ISSN: 0041-0101</identifier><identifier>EISSN: 1879-3150</identifier><identifier>DOI: 10.1016/j.toxicon.2010.11.018</identifier><identifier>PMID: 21147144</identifier><identifier>CODEN: TOXIA6</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Animal poisons toxicology. Antivenoms ; Animals ; Araneae ; Biological and medical sciences ; Blood Coagulation - drug effects ; casein ; collagen ; crosslinking ; edema ; EDTA (chelating agent) ; ethylene glycol tetraacetic acid ; Female ; fibrin ; Fibrino(geno)lytic enzyme ; fibrinogen ; Fibrinogen - chemistry ; fibronectins ; gel chromatography ; gelatin ; Hag-protease-II ; hemostasis ; Hemostasis - drug effects ; Hippasa agelenoides ; Humans ; iodoacetic acid ; ion exchange chromatography ; matrix-assisted laser desorption-ionization mass spectrometry ; Medical sciences ; molecular weight ; Platelet aggregation ; Platelet Aggregation - drug effects ; Serine Endopeptidases - chemistry ; Serine Endopeptidases - isolation & purification ; Serine Endopeptidases - pharmacology ; serine protease ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spider venom ; Spider Venoms - enzymology ; Spiders - enzymology ; Toxicology ; venoms</subject><ispartof>Toxicon (Oxford), 2011-02, Vol.57 (2), p.248-258</ispartof><rights>2010 Elsevier Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c450t-89ef459cc38b8a8665ffcd6f31c3c80e3b3343870dcb36716e6448c665d4bd8e3</citedby><cites>FETCH-LOGICAL-c450t-89ef459cc38b8a8665ffcd6f31c3c80e3b3343870dcb36716e6448c665d4bd8e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.toxicon.2010.11.018$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23834646$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21147144$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Devaraja, S.</creatorcontrib><creatorcontrib>Girish, K.S.</creatorcontrib><creatorcontrib>Gowtham, Y.N.J.</creatorcontrib><creatorcontrib>Kemparaju, K.</creatorcontrib><title>The Hag-protease-II is a fibrin(ogen)ase from Hippasa agelenoides spider venom gland extract: Purification, characterization and its role in hemostasis</title><title>Toxicon (Oxford)</title><addtitle>Toxicon</addtitle><description>The current study describes the biochemical, biophysical and pharmacological properties of Hag-protease-II from Hippasa agelenoides spider venom gland extract. The Hag-protease-II was purified to homogeneity using gel filtration and ion-exchange chromatography. The molecular mass was found to be 28.749 kDa by MALDI-TOF mass spectrometry. PMSF abolished the activity while EDTA, EGTA, IAA and 1, 10-phenanthrolene did not. Hag-protease-II hydrolyzed casein, fibrinogen and fibrin, however it did not hydrolyze gelatin, fibronectin and collagen types- I and IV. It was non-lethal and devoid of hemorrhagic, myotoxic and edema forming activities. It dose dependently reduced re-calcification time of citrated human plasma. Strikingly; the Hag-protease-II coagulated the factor X deficient congenital human plasma. It hydrolyzed Bβ-chain but, did not degrade Aα- and γ-chains of fibrinogen while, it hydrolyzed α-polymer and α-chain but not the β-chain and γ–γ dimers of partially cross-linked fibrin clot. The Hag-protease-II induced aggregation of human platelets in PRP dose dependently, however it did not interfere in collagen induced aggregation of PRP and washed human platelets.</description><subject>Animal poisons toxicology. Antivenoms</subject><subject>Animals</subject><subject>Araneae</subject><subject>Biological and medical sciences</subject><subject>Blood Coagulation - drug effects</subject><subject>casein</subject><subject>collagen</subject><subject>crosslinking</subject><subject>edema</subject><subject>EDTA (chelating agent)</subject><subject>ethylene glycol tetraacetic acid</subject><subject>Female</subject><subject>fibrin</subject><subject>Fibrino(geno)lytic enzyme</subject><subject>fibrinogen</subject><subject>Fibrinogen - chemistry</subject><subject>fibronectins</subject><subject>gel chromatography</subject><subject>gelatin</subject><subject>Hag-protease-II</subject><subject>hemostasis</subject><subject>Hemostasis - drug effects</subject><subject>Hippasa agelenoides</subject><subject>Humans</subject><subject>iodoacetic acid</subject><subject>ion exchange chromatography</subject><subject>matrix-assisted laser desorption-ionization mass spectrometry</subject><subject>Medical sciences</subject><subject>molecular weight</subject><subject>Platelet aggregation</subject><subject>Platelet Aggregation - drug effects</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - isolation & purification</subject><subject>Serine Endopeptidases - pharmacology</subject><subject>serine protease</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Spider venom</subject><subject>Spider Venoms - enzymology</subject><subject>Spiders - enzymology</subject><subject>Toxicology</subject><subject>venoms</subject><issn>0041-0101</issn><issn>1879-3150</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdGO1CAUhonRuLOjj6ByY9TEjjBQSr0xZqPOJJto4u41ofTQYdKWLjCbXV_E15U6o156dcLPd_jP4UfoGSUrSqh4t18lf-eMH1drMmt0Rah8gBZUVnXBaEkeogUhnBb5lp6h8xj3hBAma_EYna0p5RXlfIF-Xu0Ab3RXTMEn0BGK7Ra7iDW2rglufO07GN9kHdvgB7xx06SjxrqDHkbvWog4TrkEfJvPA-56PbYY7lLQJr3H3w7BWWd0cn58i81OzzIE9-O3gmfWpYiD7wG7Ee9g8DHp6OIT9MjqPsLTU12i68-fri42xeXXL9uLj5eF4SVJhazB8rI2hslGailEaa1phWXUMCMJsIYxzmRFWtMwUVEBgnNpMtfyppXAlujV8d28_80BYlKDiwb6vAb4Q1RScFZXgolMlkfSBB9jAKum4AYd7hUlao5E7dUpEjVHoihVOZLc9_zkcGgGaP92_ckgAy9PgI5G9zbo0bj4j2OSccHnAV4cOau90l3IzPX37FSSbF6vc7hL9OFIQP6xWwdBReNgNNC6ACap1rv_DPsL7cK4Kw</recordid><startdate>20110201</startdate><enddate>20110201</enddate><creator>Devaraja, S.</creator><creator>Girish, K.S.</creator><creator>Gowtham, Y.N.J.</creator><creator>Kemparaju, K.</creator><general>Elsevier Ltd</general><general>Elsevier</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>7SS</scope><scope>7U7</scope><scope>C1K</scope></search><sort><creationdate>20110201</creationdate><title>The Hag-protease-II is a fibrin(ogen)ase from Hippasa agelenoides spider venom gland extract: Purification, characterization and its role in hemostasis</title><author>Devaraja, S. ; Girish, K.S. ; Gowtham, Y.N.J. ; Kemparaju, K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-89ef459cc38b8a8665ffcd6f31c3c80e3b3343870dcb36716e6448c665d4bd8e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animal poisons toxicology. Antivenoms</topic><topic>Animals</topic><topic>Araneae</topic><topic>Biological and medical sciences</topic><topic>Blood Coagulation - drug effects</topic><topic>casein</topic><topic>collagen</topic><topic>crosslinking</topic><topic>edema</topic><topic>EDTA (chelating agent)</topic><topic>ethylene glycol tetraacetic acid</topic><topic>Female</topic><topic>fibrin</topic><topic>Fibrino(geno)lytic enzyme</topic><topic>fibrinogen</topic><topic>Fibrinogen - chemistry</topic><topic>fibronectins</topic><topic>gel chromatography</topic><topic>gelatin</topic><topic>Hag-protease-II</topic><topic>hemostasis</topic><topic>Hemostasis - drug effects</topic><topic>Hippasa agelenoides</topic><topic>Humans</topic><topic>iodoacetic acid</topic><topic>ion exchange chromatography</topic><topic>matrix-assisted laser desorption-ionization mass spectrometry</topic><topic>Medical sciences</topic><topic>molecular weight</topic><topic>Platelet aggregation</topic><topic>Platelet Aggregation - drug effects</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Endopeptidases - isolation & purification</topic><topic>Serine Endopeptidases - pharmacology</topic><topic>serine protease</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Spider venom</topic><topic>Spider Venoms - enzymology</topic><topic>Spiders - enzymology</topic><topic>Toxicology</topic><topic>venoms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Devaraja, S.</creatorcontrib><creatorcontrib>Girish, K.S.</creatorcontrib><creatorcontrib>Gowtham, Y.N.J.</creatorcontrib><creatorcontrib>Kemparaju, K.</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>Entomology Abstracts (Full archive)</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Toxicon (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Devaraja, S.</au><au>Girish, K.S.</au><au>Gowtham, Y.N.J.</au><au>Kemparaju, K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Hag-protease-II is a fibrin(ogen)ase from Hippasa agelenoides spider venom gland extract: Purification, characterization and its role in hemostasis</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>2011-02-01</date><risdate>2011</risdate><volume>57</volume><issue>2</issue><spage>248</spage><epage>258</epage><pages>248-258</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><coden>TOXIA6</coden><abstract>The current study describes the biochemical, biophysical and pharmacological properties of Hag-protease-II from Hippasa agelenoides spider venom gland extract. The Hag-protease-II was purified to homogeneity using gel filtration and ion-exchange chromatography. The molecular mass was found to be 28.749 kDa by MALDI-TOF mass spectrometry. PMSF abolished the activity while EDTA, EGTA, IAA and 1, 10-phenanthrolene did not. Hag-protease-II hydrolyzed casein, fibrinogen and fibrin, however it did not hydrolyze gelatin, fibronectin and collagen types- I and IV. It was non-lethal and devoid of hemorrhagic, myotoxic and edema forming activities. It dose dependently reduced re-calcification time of citrated human plasma. Strikingly; the Hag-protease-II coagulated the factor X deficient congenital human plasma. It hydrolyzed Bβ-chain but, did not degrade Aα- and γ-chains of fibrinogen while, it hydrolyzed α-polymer and α-chain but not the β-chain and γ–γ dimers of partially cross-linked fibrin clot. The Hag-protease-II induced aggregation of human platelets in PRP dose dependently, however it did not interfere in collagen induced aggregation of PRP and washed human platelets.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>21147144</pmid><doi>10.1016/j.toxicon.2010.11.018</doi><tpages>11</tpages></addata></record> |
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| subjects | Animal poisons toxicology. Antivenoms Animals Araneae Biological and medical sciences Blood Coagulation - drug effects casein collagen crosslinking edema EDTA (chelating agent) ethylene glycol tetraacetic acid Female fibrin Fibrino(geno)lytic enzyme fibrinogen Fibrinogen - chemistry fibronectins gel chromatography gelatin Hag-protease-II hemostasis Hemostasis - drug effects Hippasa agelenoides Humans iodoacetic acid ion exchange chromatography matrix-assisted laser desorption-ionization mass spectrometry Medical sciences molecular weight Platelet aggregation Platelet Aggregation - drug effects Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification Serine Endopeptidases - pharmacology serine protease Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spider venom Spider Venoms - enzymology Spiders - enzymology Toxicology venoms |
| title | The Hag-protease-II is a fibrin(ogen)ase from Hippasa agelenoides spider venom gland extract: Purification, characterization and its role in hemostasis |
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