dc.creatorPando, S C
dc.creatorOliva, M L
dc.creatorSampaio, C A
dc.creatorDi Ciero, L
dc.creatorNovello, J C
dc.creatorMarangoni, S
dc.date2001-Jul
dc.date2015-11-27T12:29:18Z
dc.date2015-11-27T12:29:18Z
dc.date.accessioned2018-03-29T00:56:01Z
dc.date.available2018-03-29T00:56:01Z
dc.identifierPhytochemistry. v. 57, n. 5, p. 625-31, 2001-Jul.
dc.identifier0031-9422
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11397427
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195017
dc.identifier11397427
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295250
dc.descriptionA serine proteinase inhibitor was purified from Delonix regia seeds a Leguminosae tree of the Caesalpinioideae subfamily. The inhibitor named DrTI, inactivated trypsin and human plasma kallikrein with K(i )values 2.19x10(-8) M and 5.25 nM, respectively. Its analysis by SDS-PAGE 10-20% showed that the inhibitor is a protein with a single polypeptide chain of M(r) 22 h Da. The primary sequence of the inhibitor was determined by Edman degradation, thus indicating that it contained 185 amino acids and showed that it belongs to the Kunitz type family; however, its reactive site did not contain Arg or Lys at the putative reactive site (position 63, SbTI numbering) or it was displaced when compared to other Kunitz-type inhibitors.
dc.description57
dc.description625-31
dc.languageeng
dc.relationPhytochemistry
dc.relationPhytochemistry
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectChromatography, Gel
dc.subjectChromatography, High Pressure Liquid
dc.subjectChromatography, Ion Exchange
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectFabaceae
dc.subjectMolecular Sequence Data
dc.subjectPeptides
dc.subjectPlant Proteins
dc.subjectPlants, Medicinal
dc.subjectSeeds
dc.subjectSequence Homology, Amino Acid
dc.subjectTrypsin Inhibitors
dc.titlePrimary Sequence Determination Of A Kunitz Inhibitor Isolated From Delonix Regia Seeds.
dc.typeArtículos de revistas


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