Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194040
Type: Artigo de periódico
Title: Trypanosoma Brucei: Ecto-phosphatase Activity Present On The Surface Of Intact Procyclic Forms.
Author: Fernandes, E C
Meyer-Fernandes, J R
Silva-Neto, M A
Vercesi, A E
Abstract: The results presented in this paper indicate that procyclic forms of Trypanosoma brucei possess a phosphatase activity detected in the external cell surface able to hydrolyze about 0.7 nmol.mg-1.min-1 p-nitrophenylphosphate. A faster rate of hydrolysis was observed when membrane-enriched fractions were used. This activity is weakly sensitive to 1 mM NaF, 10 mM tartrate and 10 mM levamizole but strongly inhibited by 0.1 mM vanadate. Inhibition by both NaF and vanadate have a competitive character. This phosphatase activity decreases by increasing the pH from 6.8 to 8.4, a pH range in which cell viability was maintained during at least 1 hour. In the membrane-enriched fractions this phosphatase activity showed to be an acid phosphatase. In addition, intact cells could catalyze the dephosphorylation of [32P]phosphocasein phosphorylated at serine and threonine residues.
Subject: 4-nitrophenylphosphatase
Animals
Cell Membrane
Chloromercuribenzoates
Enzyme Inhibitors
Hydrogen-ion Concentration
Kinetics
Levamisole
Phosphoric Monoester Hydrolases
Sodium Fluoride
Tartrates
Tetramisole
Trypanosoma Brucei Brucei
Vanadates
P-chloromercuribenzoic Acid
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/9232891
Date Issue: -1-Uns- -1
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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