dc.creatorAoyama, H
dc.creatorCavagis, A D
dc.creatorTaga, E M
dc.creatorFerreira, C V
dc.date2001-Sep
dc.date2015-11-27T12:28:59Z
dc.date2015-11-27T12:28:59Z
dc.date.accessioned2018-03-29T00:55:22Z
dc.date.available2018-03-29T00:55:22Z
dc.identifierPhytochemistry. v. 58, n. 2, p. 221-5, 2001-Sep.
dc.identifier0031-9422
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11551542
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194845
dc.identifier11551542
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295078
dc.descriptionThe effects of two lectins concanavalin A (conA) and soybean agglutinin, on soybean seed acid phosphatase activity were investigated using p-nitrophenylphosphate (pNPP), pyrophosphate (PPi) and phosphoenolpyruvate (PEP) as substrates. Of the four acid phosphatase isoforms (AP1, AP2, AP3A and AP3B) purified from soybean seeds, only AP1 was activated 40 and 60% by conA and soybean agglutinin, respectively. Both lectins affected some of the kinetic parameters of AP1. The activation by lectins was not affected by 1 mM Ca2+ or Mn2+ but glucose and methylmannopyranoside (100 mM) prevented activation by conA. Under the same conditions, galactose had no effect. These results suggest that plant acid phosphatases may be regulated by lectins, the effects vary according to the substrate used.
dc.description58
dc.description221-5
dc.languageeng
dc.relationPhytochemistry
dc.relationPhytochemistry
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAcid Phosphatase
dc.subjectHydrolysis
dc.subjectLectins
dc.subjectPlant Lectins
dc.subjectSeeds
dc.subjectSoybeans
dc.subjectSubstrate Specificity
dc.titleEndogenous Lectin As A Possible Regulator Of The Hydrolysis Of Physiological Substrates By Soybean Seed Acid Phosphatase.
dc.typeArtículos de revistas


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