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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleAcid Phosphatase Activities During The Germination Of Glycine Max Seeds.pt_BR
dc.contributor.authordos Prazeres, Janaina Nicanuziapt_BR
dc.contributor.authorFerreira, Carmen Veríssimapt_BR
dc.contributor.authorAoyama, Hiroshipt_BR
unicamp.authorJanaina Nicanuzia dos Prazeres, Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas, UNICAMP, Cidade Universitária, CP 6109, 13083-970 Campinas, São Paulo, Brazil.pt_BR
unicamp.author.externalCarmen Veríssima Ferreira,pt
unicamp.author.externalHiroshi Aoyama,pt
dc.subjectAcid Phosphatasept_BR
dc.subjectDarknesspt_BR
dc.subjectGerminationpt_BR
dc.subjectHypocotylpt_BR
dc.subjectKineticspt_BR
dc.subjectNitrophenolspt_BR
dc.subjectOrganophosphatespt_BR
dc.subjectOrganophosphorus Compoundspt_BR
dc.subjectPhosphatespt_BR
dc.subjectPlant Rootspt_BR
dc.subjectSeedspt_BR
dc.subjectSoybeanspt_BR
dc.subjectSubstrate Specificitypt_BR
dc.subjectTemperaturept_BR
dc.description.abstractIn this paper, we describe a study concerning the determination of some characteristics of soybean seedlings and the detection of acid phosphatase activities towards different substrates during the germination. Enzyme activities with p-nitrophenylphosphate (pNPP) and inorganic pyrophosphate (PPi) as substrates were detected from the 5th and 7th days after germination, respectively. Acid phosphatase activities with tyrosine phosphate (TyrP), glucose-6-phosphate (G6P) and phosphoenol pyruvate (PEP) were also observed but to a lesser extent. Under the same conditions, no enzyme activity was detected with phytic acid (PhyAc) as substrate. The appearance of phosphatase activity was coincident with the decrease of inorganic phosphate content during germination; over the same period, the protein content increased up to the 5th day, decreased until the 8th day, and remained constant after this period. Relative to phosphatase activity in the cotyledons, the activities detected in the hypocotyl and roots were 82% and 38%, respectively. During storage the enzyme maintained about 63% of its activity for 3 months at 5 degrees C. The specificity constant (Vmax/Km) values for pNPP and PPi were 212 and 64 mu kat mM-1 mg-1, respectively. Amongst the substrates tested, PPi could be a potential physiological substrate for acid phosphatase during the germination of soybean seeds.en
dc.relation.ispartofPlant Physiology And Biochemistry : Ppb / Société Française De Physiologie Végétalept_BR
dc.relation.ispartofabbreviationPlant Physiol. Biochem.pt_BR
dc.date.issued2004-Janpt_BR
dc.identifier.citationPlant Physiology And Biochemistry : Ppb / Société Française De Physiologie Végétale. v. 42, n. 1, p. 15-20, 2004-Jan.pt_BR
dc.language.isoengpt_BR
dc.description.volume42pt_BR
dc.description.firstpage15-20pt_BR
dc.rightsfechadopt_BR
dc.rights.holderpt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn0981-9428pt_BR
dc.identifier.doipt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/15061079pt_BR
dc.date.available2015-11-27T12:58:02Z-
dc.date.accessioned2015-11-27T12:58:02Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T12:58:02Z (GMT). No. of bitstreams: 1 pmed_15061079.pdf: 238834 bytes, checksum: badd18f6bf618eafe85784dfda28a816 (MD5) Previous issue date: 2004en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195758-
dc.identifier.idPubmed15061079pt_BR
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