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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
KeywordsBowman--Birk
Dithiothreitol
Leguminous
Phaseolus vulgaris
Issue Date2014
PublisherInforma Healthcare. The Journal's web site is located at http://www.tandf.co.uk/journals/titles/14756366.asp
Citation
Journal of Enzyme Inhibition and Medicinal Chemistry, 2014, v. 29 n. 4, p. 485-490 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
ISSN
2023 Impact Factor: 5.6
2023 SCImago Journal Rankings: 0.949
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, YS-
dc.contributor.authorZhang, Y-
dc.contributor.authorSze, SCW-
dc.contributor.authorNg, TB-
dc.date.accessioned2014-03-07T04:32:24Z-
dc.date.available2014-03-07T04:32:24Z-
dc.date.issued2014-
dc.identifier.citationJournal of Enzyme Inhibition and Medicinal Chemistry, 2014, v. 29 n. 4, p. 485-490-
dc.identifier.issn1475-6366-
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.-
dc.languageeng-
dc.publisherInforma Healthcare. The Journal's web site is located at http://www.tandf.co.uk/journals/titles/14756366.asp-
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistry-
dc.rightsJournal of Enzyme Inhibition and Medicinal Chemistry. Copyright © Informa Healthcare.-
dc.subjectBowman--Birk-
dc.subjectDithiothreitol-
dc.subjectLeguminous-
dc.subjectPhaseolus vulgaris-
dc.titleA thermostable trypsin inhibitor with antiproliferative activity from small pinto beans-
dc.typeArticle-
dc.identifier.emailChan, YS: cys911@hku.hk-
dc.identifier.emailZhang, Y: ybzhang@hku.hk-
dc.identifier.emailSze, SCW: stephens@hku.hk-
dc.identifier.authorityZhang, Y=rp01410-
dc.identifier.authoritySze, SCW=rp00514-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.3109/14756366.2013.805756-
dc.identifier.pmid23859150-
dc.identifier.scopuseid_2-s2.0-84904361953-
dc.identifier.hkuros228206-
dc.identifier.hkuros245958-
dc.identifier.volume29-
dc.identifier.issue4-
dc.identifier.spage485-
dc.identifier.epage490-
dc.identifier.isiWOS:000340106800004-
dc.publisher.placeUnited Kingdom-
dc.identifier.issnl1475-6366-

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