Soybean Seed Acid Phosphatases: Unusual Optimum Temperature And Thermal Stability Studies.

dc.creatorFerreira, C V
dc.creatorGranjeiro, J M
dc.creatorTaga, E M
dc.creatorAoyama, H
dc.date1998-Jan
dc.date2015-11-27T12:19:08Z
dc.date2015-11-27T12:19:08Z
dc.date.accessioned2018-03-29T00:52:36Z
dc.date.available2018-03-29T00:52:36Z
dc.identifierBiochemical And Biophysical Research Communications. v. 242, n. 2, p. 282-6, 1998-Jan.
dc.identifier0006-291X
dc.identifier10.1006/bbrc.1997.7954
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9446785
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194126
dc.identifier9446785
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294359
dc.descriptionIn contrast to other acid phosphatases, four cytoplasmic isoforms (AP1, AP2, AP3A, and AP3B) purified from mature soybean seeds presented high activities at temperatures above 80 degrees C, when p-nitrophenylphosphate (p-NPP) was utilized as substrate. However, with tyrosine phosphate and inorganic pyrophosphate as substrates, maximum activities were observed at temperature of 60 degrees C during 10 min reaction. In the absence of substrate, enzymes lost only 20% activity after 60 min at 60 degrees C; the isoforms AP3A and AP3B retained 30% of activity at 70 degrees C after 60 min and all the isoforms were inactivated at 80 degrees C, after 5 min. Thermal inactivation studies indicated that the soybean enzymes showed different temperature dependences in relation to most plant acid phosphatases. A best protective effect was observed when the isoforms were preincubated, at 70 degrees C, with phosphate (10 mM) and p-nitrophenol (10 mM) which indicates that the enzyme inactivation was prevented only in the presence of both reaction products.
dc.description242
dc.description282-6
dc.languageeng
dc.relationBiochemical And Biophysical Research Communications
dc.relationBiochem. Biophys. Res. Commun.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAcid Phosphatase
dc.subjectCytoplasm
dc.subjectDiphosphates
dc.subjectEnzyme Stability
dc.subjectIsoenzymes
dc.subjectNitrophenols
dc.subjectOctoxynol
dc.subjectOrganophosphorus Compounds
dc.subjectPhosphates
dc.subjectPhosphotyrosine
dc.subjectPlant Proteins
dc.subjectSeeds
dc.subjectSoybeans
dc.subjectTemperature
dc.subjectVanadates
dc.titleSoybean Seed Acid Phosphatases: Unusual Optimum Temperature And Thermal Stability Studies.
dc.typeArtículos de revistas


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