Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom
A thrombin-like enzyme (termed albolabrase) was isolated in purified form from the venom of Cryptelytrops albolabris (white-lipped tree viper) using high performance anion ion exchange and gel filtration chromatography. The molecular mass of albolabrase was 33.7 kDa as determined by SDS-PAGE and 35....
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2012
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| author | Tan, N.H. Fung, S.Y. Yap, Y.H.Y. |
| author_facet | Tan, N.H. Fung, S.Y. Yap, Y.H.Y. |
| author_sort | Tan, N.H. |
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| content_provider | Universiti Malaya |
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| description | A thrombin-like enzyme (termed albolabrase) was isolated in purified form from the venom of Cryptelytrops albolabris (white-lipped tree viper) using high performance anion ion exchange and gel filtration chromatography. The molecular mass of albolabrase was 33.7 kDa as determined by SDS-PAGE and 35.8 kDa as determined by Superose gel filtration chromatography. The N-terminal sequence was determined to be VVGGDECNINE which is homologous to many snake venom thrombin-like enzymes. Albolabrase exhibits both arginine ester hydrolase and arginine amidase activities and the enzyme is fastidious towards tripeptide chromogenic anilide substrates. The fibrinogen clotting activity was optimum at 3 mg/mL bovine fibrinogen, and showed distinct species differences in the following decreasing order: bovine fibrinogen > dog fibrinogen � human fibrinogen > goat fibrinogen. The enzyme failed to clot both rabbit and cat fibrinogens. Reversed-phase HPLC analysis on the breakdown products of fibrinogenolytic action of albolabrase indicated that the enzyme belongs to the AB class of snake venom thrombin-like enzyme. In the indirect ELISA, IgG anti-albolabrase reacted extensively with most crotalid venoms, except with Tropidolaemus wagleri and Calloselasma rhodostoma venoms. The double sandwich ELISA, however, showed that anti-albolabrase reacted strongly only with venoms from the Trimeresurus complex, and that the results support the proposed new taxonomy changes concerning the Trimeresurus complex. |
| format | Article |
| id | my.um.eprints-3696 |
| institution | Universiti Malaya |
| language | en |
| publishDate | 2012 |
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| spelling | my.um.eprints-36962012-09-25T02:25:14Z http://eprints.um.edu.my/3696/ Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom Tan, N.H. Fung, S.Y. Yap, Y.H.Y. R Medicine A thrombin-like enzyme (termed albolabrase) was isolated in purified form from the venom of Cryptelytrops albolabris (white-lipped tree viper) using high performance anion ion exchange and gel filtration chromatography. The molecular mass of albolabrase was 33.7 kDa as determined by SDS-PAGE and 35.8 kDa as determined by Superose gel filtration chromatography. The N-terminal sequence was determined to be VVGGDECNINE which is homologous to many snake venom thrombin-like enzymes. Albolabrase exhibits both arginine ester hydrolase and arginine amidase activities and the enzyme is fastidious towards tripeptide chromogenic anilide substrates. The fibrinogen clotting activity was optimum at 3 mg/mL bovine fibrinogen, and showed distinct species differences in the following decreasing order: bovine fibrinogen > dog fibrinogen � human fibrinogen > goat fibrinogen. The enzyme failed to clot both rabbit and cat fibrinogens. Reversed-phase HPLC analysis on the breakdown products of fibrinogenolytic action of albolabrase indicated that the enzyme belongs to the AB class of snake venom thrombin-like enzyme. In the indirect ELISA, IgG anti-albolabrase reacted extensively with most crotalid venoms, except with Tropidolaemus wagleri and Calloselasma rhodostoma venoms. The double sandwich ELISA, however, showed that anti-albolabrase reacted strongly only with venoms from the Trimeresurus complex, and that the results support the proposed new taxonomy changes concerning the Trimeresurus complex. 2012 Article PeerReviewed application/pdf en http://eprints.um.edu.my/3696/1/Isolation_and_characterization_of_the_thrombin-like_enzyme_from_Cryptelytrops_albolabris_%28white-lipped_tree_viper%29_venom..pdf Tan, N.H. and Fung, S.Y. and Yap, Y.H.Y. (2012) Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 161 (1). pp. 79-85. ISSN 1096-4959, |
| spellingShingle | R Medicine Tan, N.H. Fung, S.Y. Yap, Y.H.Y. Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom |
| title | Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom |
| title_full | Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom |
| title_fullStr | Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom |
| title_full_unstemmed | Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom |
| title_short | Isolation and characterization of the thrombin-like enzyme from Cryptelytrops albolabris (white-lipped tree viper) venom |
| title_sort | isolation and characterization of the thrombin-like enzyme from cryptelytrops albolabris (white-lipped tree viper) venom |
| topic | R Medicine |
| url | http://eprints.um.edu.my/3696/1/Isolation_and_characterization_of_the_thrombin-like_enzyme_from_Cryptelytrops_albolabris_%28white-lipped_tree_viper%29_venom..pdf http://eprints.um.edu.my/3696/ |
| url_provider | http://eprints.um.edu.my/ |