Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library
Atroxase, isolated from the venom of Crotalus atrox (western diamondback rattlesnake), is a nonhemorrhagic protease which has fibrinolytic activity in vivo. The primary structure of atroxase was deduced from the cDNA encoding the atroxase protein. The venom glands of Crotalus atrox were used to prep...
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th-mahidol.172522018-07-04T13:52:21Z Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library Brenda J. Baker Sirima Wongvibulsin Jennifer Nyborg Anthony T. Tu Colorado State University Mahidol University Biochemistry, Genetics and Molecular Biology Atroxase, isolated from the venom of Crotalus atrox (western diamondback rattlesnake), is a nonhemorrhagic protease which has fibrinolytic activity in vivo. The primary structure of atroxase was deduced from the cDNA encoding the atroxase protein. The venom glands of Crotalus atrox were used to prepare a cDNA library. Degenerate oligonucleotides were synthesized based on the partial amino acid sequence of atroxase and were used as primers in the polymerase chain reaction to amplify overlapping cDNA fragments from the C. atrox cDNA library. The resulting cDNA fragments were subcloned, sequenced, and translated. The final nucleotide sequence shows high homology to previously described primary structures of nonhemorrhagic fibrinolytic proteases isolated from snake venom. © 1995 by Academic Press, Inc. 2018-07-04T06:52:21Z 2018-07-04T06:52:21Z 1995-01-01 Article Archives of Biochemistry and Biophysics. Vol.317, No.2 (1995), 357-364 10.1006/abbi.1995.1175 00039861 2-s2.0-0028953293 https://repository.li.mahidol.ac.th/handle/123456789/17252 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0028953293&origin=inward |
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Biochemistry, Genetics and Molecular Biology Brenda J. Baker Sirima Wongvibulsin Jennifer Nyborg Anthony T. Tu Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library |
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Atroxase, isolated from the venom of Crotalus atrox (western diamondback rattlesnake), is a nonhemorrhagic protease which has fibrinolytic activity in vivo. The primary structure of atroxase was deduced from the cDNA encoding the atroxase protein. The venom glands of Crotalus atrox were used to prepare a cDNA library. Degenerate oligonucleotides were synthesized based on the partial amino acid sequence of atroxase and were used as primers in the polymerase chain reaction to amplify overlapping cDNA fragments from the C. atrox cDNA library. The resulting cDNA fragments were subcloned, sequenced, and translated. The final nucleotide sequence shows high homology to previously described primary structures of nonhemorrhagic fibrinolytic proteases isolated from snake venom. © 1995 by Academic Press, Inc. |
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Colorado State University |
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Colorado State University Brenda J. Baker Sirima Wongvibulsin Jennifer Nyborg Anthony T. Tu |
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Article |
author |
Brenda J. Baker Sirima Wongvibulsin Jennifer Nyborg Anthony T. Tu |
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Brenda J. Baker |
title |
Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library |
title_short |
Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library |
title_full |
Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library |
title_fullStr |
Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library |
title_full_unstemmed |
Nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a Crotalus atrox venom gland cDNA library |
title_sort |
nucleotide sequence encoding the snake venom fibrinolytic enzyme atroxase obtained from a crotalus atrox venom gland cdna library |
publishDate |
2018 |
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https://repository.li.mahidol.ac.th/handle/123456789/17252 |
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1763496929706115072 |