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Article: Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom

TitlePurification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom
Authors
Issue Date2004
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1
Citation
Acta Crystallographica Section D: Biological Crystallography, 2004, v. 60 n. 5, p. 974-977 How to Cite?
AbstractA snake-venom protein named AHP-LAAO has been purified from Agkistrodon halys pallas venom using four-stage chromatography. AHP-LAAO is a novel member of the snake-venom L-amino-acid oxidase family. Its amino-acid sequence shows high homology to other members of this family. For L-leucine, the values of k cat and K M are 31.1 s -1 and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce apoptosis of cultured Hela cells. Two sets of diffraction data with similar resolution limits (about 2.5 Å) were collected independently at MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute of High Energy Physics, Beijing, China). The crystals belong to space group I2 13, with unit-cell parameter a = 169.31 Å, corresponding to one molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 Å 3 Da -1. The final structural model is similar to that of L-amino-acid oxidase from Calloselasma rhodostoma venom. © 2004 International Union of Crystallography. Printed in Denmark - all rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91949
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Hen_HK
dc.contributor.authorTeng, Men_HK
dc.contributor.authorNiu, Len_HK
dc.contributor.authorWang, Yen_HK
dc.contributor.authorWang, Yen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHuang, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorDong, Yen_HK
dc.contributor.authorLiu, Pen_HK
dc.date.accessioned2010-09-17T10:31:25Z-
dc.date.available2010-09-17T10:31:25Z-
dc.date.issued2004en_HK
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 2004, v. 60 n. 5, p. 974-977en_HK
dc.identifier.issn0907-4449en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91949-
dc.description.abstractA snake-venom protein named AHP-LAAO has been purified from Agkistrodon halys pallas venom using four-stage chromatography. AHP-LAAO is a novel member of the snake-venom L-amino-acid oxidase family. Its amino-acid sequence shows high homology to other members of this family. For L-leucine, the values of k cat and K M are 31.1 s -1 and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce apoptosis of cultured Hela cells. Two sets of diffraction data with similar resolution limits (about 2.5 Å) were collected independently at MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute of High Energy Physics, Beijing, China). The crystals belong to space group I2 13, with unit-cell parameter a = 169.31 Å, corresponding to one molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 Å 3 Da -1. The final structural model is similar to that of L-amino-acid oxidase from Calloselasma rhodostoma venom. © 2004 International Union of Crystallography. Printed in Denmark - all rights reserved.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1en_HK
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallographyen_HK
dc.titlePurification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venomen_HK
dc.typeArticleen_HK
dc.identifier.emailZhang, H: hzhang20@hku.hken_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityZhang, H=rp00306en_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S0907444904000046en_HK
dc.identifier.scopuseid_2-s2.0-12344308486en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-12344308486&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume60en_HK
dc.identifier.issue5en_HK
dc.identifier.spage974en_HK
dc.identifier.epage977en_HK
dc.identifier.isiWOS:000220951000034-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhang, H=7409196101en_HK
dc.identifier.scopusauthoridTeng, M=7101891754en_HK
dc.identifier.scopusauthoridNiu, L=7101760477en_HK
dc.identifier.scopusauthoridWang, Y=7601496127en_HK
dc.identifier.scopusauthoridWang, Y=8548677800en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHuang, Q=7403634448en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridDong, Y=26428652500en_HK
dc.identifier.scopusauthoridLiu, P=26643498100en_HK

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