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Article: A thermostable trypsin inhibitor with antiproliferative activity from small pinto beans

TitleA thermostable trypsin inhibitor with antiproliferative activity from small pinto beans
Authors
Issue Date2013
Citation
Journal of Enzyme Inhibition and Medicinal Chemistry, 2013, v. 2013, p. 1475-6374 How to Cite?
AbstractSmall pinto bean is a cultivar of Phaseolus vulgaris. It produces a 16-kDa trypsin inhibitor that could be purified using anion exchange and size chromatography. Q-Sepharose, Mono Q and Superdex 75 columns were employed for the isolation process. Small pinto bean trypsin inhibitor demonstrated moderate pH stability (pH 2–10) and marked heat stability, with its trypsin inhibitory activity largely retained after exposure to 100 °C for half an hour. The activity was abolished in the presence of dithiothreitol, in a dose-dependent manner, implying that disulfide bonds in small pinto bean trypsin inhibitor are crucial for the activity. The trypsin inhibitor showed a blocked N-terminus. The trypsin inhibitor only slightly inhibited the viability of breast cancer MCF7 and hepatoma HepG2 cells at 125 μM.
Persistent Identifierhttp://hdl.handle.net/10722/195706
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, YSen_US
dc.contributor.authorZhang, Yen_US
dc.contributor.authorSze, CWen_US
dc.contributor.authorNg, TBen_US
dc.date.accessioned2014-03-07T04:32:24Z-
dc.date.available2014-03-07T04:32:24Z-
dc.date.issued2013en_US
dc.identifier.citationJournal of Enzyme Inhibition and Medicinal Chemistry, 2013, v. 2013, p. 1475-6374en_US
dc.identifier.urihttp://hdl.handle.net/10722/195706-
dc.description.abstractSmall pinto bean is a cultivar of Phaseolus vulgaris. It produces a 16-kDa trypsin inhibitor that could be purified using anion exchange and size chromatography. Q-Sepharose, Mono Q and Superdex 75 columns were employed for the isolation process. Small pinto bean trypsin inhibitor demonstrated moderate pH stability (pH 2–10) and marked heat stability, with its trypsin inhibitory activity largely retained after exposure to 100 °C for half an hour. The activity was abolished in the presence of dithiothreitol, in a dose-dependent manner, implying that disulfide bonds in small pinto bean trypsin inhibitor are crucial for the activity. The trypsin inhibitor showed a blocked N-terminus. The trypsin inhibitor only slightly inhibited the viability of breast cancer MCF7 and hepatoma HepG2 cells at 125 μM.en_US
dc.languageengen_US
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistryen_US
dc.titleA thermostable trypsin inhibitor with antiproliferative activity from small pinto beansen_US
dc.typeArticleen_US
dc.identifier.emailChan, YS: cys911@hku.hken_US
dc.identifier.emailZhang, Y: ybzhang@hku.hken_US
dc.identifier.emailSze, CW: stephens@hku.hken_US
dc.identifier.authorityZhang, Y=rp01410en_US
dc.identifier.authoritySze, CW=rp00514en_US
dc.identifier.doi10.3109/14756366.2013.805756en_US
dc.identifier.pmid23859150-
dc.identifier.hkuros228206en_US
dc.identifier.hkuros245958-
dc.identifier.volume2013en_US
dc.identifier.spage1475en_US
dc.identifier.epage6374en_US
dc.identifier.isiWOS:000340106800004-
dc.publisher.placeUKen_US

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