Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194126
Type: Artigo de periódico
Title: Soybean Seed Acid Phosphatases: Unusual Optimum Temperature And Thermal Stability Studies.
Author: Ferreira, C V
Granjeiro, J M
Taga, E M
Aoyama, H
Abstract: In 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.
Subject: Acid Phosphatase
Cytoplasm
Diphosphates
Enzyme Stability
Isoenzymes
Nitrophenols
Octoxynol
Organophosphorus Compounds
Phosphates
Phosphotyrosine
Plant Proteins
Seeds
Soybeans
Temperature
Vanadates
Rights: fechado
Identifier DOI: 10.1006/bbrc.1997.7954
Address: http://www.ncbi.nlm.nih.gov/pubmed/9446785
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

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