Fabian Bracco

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The activity of cathepsin D on hemoglobin and on cytoplasmic tubulin was measured in brain preparations at different ages--in newborn, 10- and 21-day-old, and young adult rats. Enzyme activity increased after birth, reaching a maximum at around 21 days, and then declined. This increase was not parallel with decreased turnover of proteins during development,(More)
—This paper proposes the first attempt for semi-automatic screening and identification of red imported fire ants (Solenopsis invicta) in Australia. As an exotic ant species to Australia, fire ants were imported from South America in 2001 and have since been regarded as dangerous pests that could severely damage the environment and many industries. We(More)
In a continuing study of control processes of cerebral protein catabolism we compared the activity of cathepsin D from three sources (rat brain, bovine brain, and bovine spleen) on purified CNS proteins (tubulin, actin, calmodulin, S-100 and glial fibrillary acidic protein). The pH optimum was 5 for hydrolysis with tubulin as substrate for all three enzyme(More)
The breakdown of cytoplasmic tubulin from brain (purified by ammonium sulfate fractionation and DEAE cellulose chromatography) by cathepsin D from brain (purified by ammonium sulfate fractionation and pepstatin Sepharose chromatography) was studied; changes in the intensity of tubulin gel bands were determined. The pH optimum of hemoglobin breakdown by(More)
In recent studies we found that cytoplasmic tubulin from brain was rapidly split by brain cathepsin D. Two pools could be established; the major portion was split at 18%/h, a minor portion at 2%/h, under our experimental circumstances. In the present work these experiments were extended to membrane-bound tubulin from brain. The membrane-bound form, in(More)
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