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Protein method for investigating mercuric reductase gene expression in aquatic environments

Article Abstract:

A calorimetric assay was developed as a method for investigating nicotinamide adenine dinucleotide phosphate (NADPH) -dependent, mercuric ion-specific oxidereductase activity in protein molecules extracted from samples from polluted aquatic ecosystems. This approach combines three important biochemical processing techniques, namely, the conservative recovery of microbial proteins straight from heterogeneous biological systems, the NADPH-dependent kinetics of mercuric reductase activity, and the titration of residual NADPH through the stoichiometric reduction of tetrazolium salts. The study's findings are discussed.

Author: Ogunseitan, O.A.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Water pollution, NAD (Coenzyme), Nicotinamide adenine dinucleotide

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Inactivation of tryptic activity by a human-derived strain of Bacteroides distasonis in the large intestines of gnotobiotic rats and mice

Article Abstract:

A human-derived Bacteroides distasonis strain inactivates tryptic activity and trypsin is undetectable in the large intestine of gnotobiotic rats and mice infected with the bacterium. However, tryptic activity in the small intestines is unaffected. The inactivation property is specific for this strain as a closely related B. distasonis strain is unable to produce the same effect.

Author: Hautefort, Isabelle, Raibaud, Pierre, Ramare, Francoise, Verhe, Frederic, Iovanna, Juan
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Physiological aspects, Observations, Bacteria, Intestines, Trypsin inhibitors, Rodents as laboratory animals, Laboratory rodents

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Single-copy green fluorescent protein gene fusions allow accurate measurement of Salmonella gene expression in vitro and during infection of mammalian cells

Article Abstract:

A reliable and flexible green fluorescent protein (GFP)-based system for measuring gene expression in individual bacterial cells is developed. The results demonstrate for the first time that single-copy GFP+ fusions reliably report gene expression in simple and complex environment.

Author: Hautefort, Isabelle, Proenca, Maria Jose, Hinton, Jay C. D.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
Science & research, Genetic aspects, Mammals

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Subjects list: Research, Proteins, Gene expression
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