Sally Muller Affonso Prado
Universidade Federal de Minas Gerais
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Featured researches published by Sally Muller Affonso Prado.
Biotechnology Progress | 2008
Fernando Fratelli; Tatiana Joly Siquini; Sally Muller Affonso Prado; Hisako Gondo Higashi; Attilio Converti; João Carlos Monteiro de Carvalho
The tetanus toxin is a neurotoxin synthesized by the bacillus Clostridium tetani that, after detoxification with formaldehyde, still exhibits antigenic and immunologic properties, hence its denomination of tetanus toxoid. Such a neurotoxin is produced by cultivation of the microorganism in vegetative form on a relatively complex specific medium containing glucose and peptone. The simultaneous effects of the starting levels of glucose (G0) and N‐Z Case TT (NZ0) as carbon and nitrogen sources, respectively, on the production of tetanus toxin have been investigated in this work in static cultivations by means of a five‐level star‐shaped experimental design and evaluated by response surface methodology (RSM) for optimization purposes. The highest final average yield of tetanus toxin (72 Lf/mL), achieved at G0 = 9.7 g/L and NZ0 = 43.5 g/L, was 80% higher than that obtained with standard cultivations (G0 = 8.0 g/L and NZ0 = 25.0 g/L).
Biotechnology and Applied Biochemistry | 2002
Elen A. Perpetuo; Luis Juliano; Sally Muller Affonso Prado; Fernando Fratelli; Irene Fernandes; Ivo Lebrun
Tetanus neurotoxin (TTx), produced by Clostridium tetani, is a two‐chain polypeptide with a heavy molecular chain (HC; 100 kDa) and a light molecular chain (LC; 50 kDa) linked by a disulphide bridge. The low‐molecular‐mass chain is classified as a zinc metalloprotease (EC 3.4.24.68) with specific hydrolysis on synaptobrevin. With the known enzymic activity for the LC of TTx, we developed a quantification method using a quenched fluorescence peptide substrate based on the synaptobrevin sequence (fragments 73–82), suitable for direct determination of the whole TTx (HC+LC) even in crude production batches, without the necessity of purification and reduction steps to isolate the LC of TTx. The rate of substrate hydrolysis was 200 nmol/min and it was totally inhibited by EDTA, anti‐recombinant fragment C antibody, and the cleavage was in a single bond (Gln‐Phe) with purified and crude TTx. Besides, ELISA applied to the anti‐TTx serum produced at our Institute showed cross‐reaction with every fraction of the crude TTx extract. Another aspect is that TTx activity depends on the storage time, reaching a maximum on day 10. The results obtained suggest that the use of the new fluorescent substrate, Abz‐synaptobrevin73–82‐EDDnp, enables easy and quick determination of TTx. It is a good alternative to some of the existing methods such as flocculation assay, and it can replace, under some conditions, the biological assays (minimal mortal dose).
Preparative Biochemistry & Biotechnology | 2007
Elen A. Perpetuo; Ivo Lebrun; Luis Juliano; Maria A. Juliano; Maria Aparecida Sakauchi; Sally Muller Affonso Prado
Abstract Proteases were identified and characterized from the culture supernatant of the C. diphtheriae and B. pertussis bacteria. The proteases were secreted in the media and detected at the end of the exponential growth phase. Activity was detected in some fluorescent substrates, based on selected protein sequences such as insuline β‐chain, bradykinin, and synaptobrevin. The proteases were purified by means of gel filtration chromatography. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) analysis of the purified proteins indicated, for the main secreted proteins, an estimated molecular mass of 30 kDa in C. diphtheriae and 69 kDa in B. pertussis culture media. The proteases were stable and presented enzymatic activity at 37°C. These proteases were not related to the main toxic compounds described in these two bacteria, but could represent good markers for the fermentation process when the enzyme activity was measured with the fluorescent substrates.
Archive | 2007
Isaias Raw; Flávia Saldanha Kubrusly; Waldely O. Dias; Maria Izabel Esteves; Noemi Furuyama; Denise Silvina Piccini Quintas Horton; Ednilse Leme; Wagner Quintilio; Maria Aparecida Sakauchi; Sally Muller Affonso Prado; Elizabeth Mendes; Hisako Gondo Higashi
Biologicals | 1994
Heloisa R. Soares; Ronaldo Luiz Nunes; Sally Muller Affonso Prado; Hisako G. Higashi; Ibrahim F. Heneine
Mem. Inst. Butantan | 1993
Fernando Fratelli; Sally Muller Affonso Prado; Mary Dalva Caparroz Vancetto; José Marcos de Oliveira; Hisako Gondo Higashi
Mem. Inst. Butantan | 1993
Sally Muller Affonso Prado; Mary Dalva Caparroz Vancetto; José Marcos de Oliveira; Fernando Fratelli; Sandra de Jesus Delgado Mathias; Hisako Gondo Higashi
Mem. Inst. Butantan | 1992
Sally Muller Affonso Prado; Mary Dalva Caparroz Vancetto; Fernando Fratelli; Michel Marie Pral; José Marcos de Oliveira; Hisako Gondo Higashi
Archive | 2007
Isaias Raw; Flávia Saldanha Kubrusly; Dmitri Iourtov; Maria Aparecida Sakauchi; Fernanda L. Santos; Elaine Darini; Noemi Furuyama; Sally Muller Affonso Prado; Hisako Gondo Higashi; Sandra de Cássia Dias
Arq. biol. tecnol | 1996
Sally Muller Affonso Prado; Mary Dalva Caparroz Vancetto; José Marcos de Oliveira; Joana Akiko Furuta; Maria Lúcia Rodrigues Gioielli; Hisako Gondo Higashi