dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorNeves, Valdir Augusto
dc.creatorLourenço, Euclides Joaquim
dc.date2014-05-27T11:20:18Z
dc.date2016-10-25T18:17:10Z
dc.date2014-05-27T11:20:18Z
dc.date2016-10-25T18:17:10Z
dc.date2001-09-01
dc.date.accessioned2017-04-06T01:00:01Z
dc.date.available2017-04-06T01:00:01Z
dc.identifierArchivos Latinoamericanos de Nutricion, v. 51, n. 3, p. 269-275, 2001.
dc.identifier0004-0622
dc.identifierhttp://hdl.handle.net/11449/66578
dc.identifierhttp://acervodigital.unesp.br/handle/11449/66578
dc.identifierS0004-06222001000300009
dc.identifierWOS:000172363800009
dc.identifier2-s2.0-0035467940
dc.identifierhttp://www.scielo.org.ve/scielo.php?pid=S0004-06222001000300009&script=sci_arttext
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/888123
dc.descriptionThe chickpea seed germination was carried out in 6 days. During the period it was observed a little variation on total nitrogen contents, however the non protein nitrogen was double. A decrease of 19.1 and 20.6% in relation to total nitrogen was observed to the total globulin and albumin fractions, respectively. The gel filtration chromatography on Sepharose CL-6B and SDS-PAGE demonstrated alterations on the distribution patterns of the albumin and total globulin fractions between the initial and the sixth day of germination suggesting the occurrence of protein degradation in the germination process.The assay for acid protease only appeared in the albumin fraction with casein and chickpea total globulin as substrates, whereas the former was more degradated than the latter, however the transformations detected in the protein fractions apppear indicated that others enzymes could be acting during the process. The trypsin inhibitor activity had a little drop after six day of germination indicating a possible increase on the digestibility of the proteins.
dc.languageeng
dc.relationArchivos Latinoamericanos de Nutrición
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectChickpea
dc.subjectCicer arietinum L.
dc.subjectGermination
dc.subjectProtein fractions
dc.subjectalbuminoid
dc.subjectglobulin
dc.subjectnitrogen
dc.subjectpeptide hydrolase
dc.subjectsepharose
dc.subjecttrypsin inhibitor
dc.subjectvegetable protein
dc.subjectchemistry
dc.subjectchickpea
dc.subjectcotyledon
dc.subjectenzymology
dc.subjectgel chromatography
dc.subjectgermination
dc.subjectgrowth, development and aging
dc.subjectmetabolism
dc.subjectplant seed
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectAlbumins
dc.subjectChromatography, Gel
dc.subjectCicer
dc.subjectCotyledon
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectGlobulins
dc.subjectNitrogen
dc.subjectPeptide Hydrolases
dc.subjectPlant Proteins
dc.subjectSeeds
dc.subjectSepharose
dc.subjectTrypsin Inhibitors
dc.titleChanges in protein fractions, trypsin inhibitor and proteolytic activity in the cotyledons of germinating chickpea
dc.typeOtro


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