A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch

R. Gao; Yong Zhang; P. Gopalakrishnakone

doi:10.1007/978-3-540-69139-6_206

A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch

R. Gao
, Yong Zhang
, P. Gopalakrishnakone

Research output: Chapters, Conference Papers, Creative and Literary Works › RGC 32 - Refereed conference paper (with host publication) › peer-review

2 Citations (Scopus)

Abstract

By using the combination of gel filtration, ion-exchange and reveres-phase chromatography, a novel trypsinlike serine proteinase was isolated from the venom of Buthus martensii Karsch and named BMK-CB. The apparent molecular weight of BMK-CB was identified as 32 kDa by SDSPAGE. The N-terminal sequence of 40 amino acids was obtained by Edman degradation. The sequence shows highest similarity to proteinase from insect source. The purified BMKCB was found to bind to the cancer cell line MCF-7 and the cell binding ability was dose-dependent. To our knowledge, BMK-CB forms the first trypsin-like serine proteinase from the scorpion venom. © 2008 Springer-Verlag.

Original language	English
Title of host publication	4th Kuala Lumpur International Conference on Biomedical Engineering 2008, Biomed 2008
Publisher	Springer Verlag
Pages	829-832
Volume	21 IFMBE
ISBN (Print)	9783540691389
DOIs	https://doi.org/10.1007/978-3-540-69139-6_206
Publication status	Published - 2008
Externally published	Yes

Publication series

Name	IFMBE Proceedings
Volume	21 IFMBE
ISSN (Print)	1680-0737

Bibliographical note

Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].

Funding

The work was funded by grant R-398-000-030-305 from A*STAR SERC (Singapore).

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Keywords

Cell binding
Purification
Scorpion venom
Serine proteinase

Access Output

10.1007/978-3-540-69139-6_206

Other Access Options

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Permanent Link

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Cite this

Gao, R., Zhang, Y., & Gopalakrishnakone, P. (2008). A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch. In 4th Kuala Lumpur International Conference on Biomedical Engineering 2008, Biomed 2008 (Vol. 21 IFMBE, pp. 829-832). (IFMBE Proceedings; Vol. 21 IFMBE). Springer Verlag. https://doi.org/10.1007/978-3-540-69139-6_206

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abstract = "By using the combination of gel filtration, ion-exchange and reveres-phase chromatography, a novel trypsinlike serine proteinase was isolated from the venom of Buthus martensii Karsch and named BMK-CB. The apparent molecular weight of BMK-CB was identified as 32 kDa by SDSPAGE. The N-terminal sequence of 40 amino acids was obtained by Edman degradation. The sequence shows highest similarity to proteinase from insect source. The purified BMKCB was found to bind to the cancer cell line MCF-7 and the cell binding ability was dose-dependent. To our knowledge, BMK-CB forms the first trypsin-like serine proteinase from the scorpion venom. {\textcopyright} 2008 Springer-Verlag.",

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A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch. / Gao, R.; Zhang, Yong; Gopalakrishnakone, P.
4th Kuala Lumpur International Conference on Biomedical Engineering 2008, Biomed 2008. Vol. 21 IFMBE Springer Verlag, 2008. p. 829-832 (IFMBE Proceedings; Vol. 21 IFMBE).

Research output: Chapters, Conference Papers, Creative and Literary Works › RGC 32 - Refereed conference paper (with host publication) › peer-review

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AU - Gopalakrishnakone, P.

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PY - 2008

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N2 - By using the combination of gel filtration, ion-exchange and reveres-phase chromatography, a novel trypsinlike serine proteinase was isolated from the venom of Buthus martensii Karsch and named BMK-CB. The apparent molecular weight of BMK-CB was identified as 32 kDa by SDSPAGE. The N-terminal sequence of 40 amino acids was obtained by Edman degradation. The sequence shows highest similarity to proteinase from insect source. The purified BMKCB was found to bind to the cancer cell line MCF-7 and the cell binding ability was dose-dependent. To our knowledge, BMK-CB forms the first trypsin-like serine proteinase from the scorpion venom. © 2008 Springer-Verlag.

AB - By using the combination of gel filtration, ion-exchange and reveres-phase chromatography, a novel trypsinlike serine proteinase was isolated from the venom of Buthus martensii Karsch and named BMK-CB. The apparent molecular weight of BMK-CB was identified as 32 kDa by SDSPAGE. The N-terminal sequence of 40 amino acids was obtained by Edman degradation. The sequence shows highest similarity to proteinase from insect source. The purified BMKCB was found to bind to the cancer cell line MCF-7 and the cell binding ability was dose-dependent. To our knowledge, BMK-CB forms the first trypsin-like serine proteinase from the scorpion venom. © 2008 Springer-Verlag.

KW - Cell binding

KW - Purification

KW - Scorpion venom

KW - Serine proteinase

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DO - 10.1007/978-3-540-69139-6_206

M3 - RGC 32 - Refereed conference paper (with host publication)

SN - 9783540691389

VL - 21 IFMBE

T3 - IFMBE Proceedings

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BT - 4th Kuala Lumpur International Conference on Biomedical Engineering 2008, Biomed 2008

PB - Springer Verlag

ER -

A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch

Abstract

Publication series

Bibliographical note

Funding

UN SDGs

Research Keywords

Access Output

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