Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/71973
Type: Artigo de periódico
Title: Soybean seed acid phosphatases: Unusual optimum temperature and thermal stability studies
Author: Ferreira, GV
Granjeiro, JM
Taga, EM
Aoyama, H
Abstract: In contrast to other acid phosphatases, four cytoplasmic isoforms (AP1, AP2, AP3A and APSB) 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 mill 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. (C) 1998 Academic Press.
Country: EUA
Editor: Academic Press Inc
Rights: fechado
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

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