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Effect of endosulfan on Azospirillum lipoferum growth, morphology, nitrogenase activity and protein binding

Article Abstract:

Endosulfan is an organochlorine acaricide which exhibits some nonspecific antimicrobial activities. An investigation was conducted to determine the effects of Endosulfan on Azospirillum lipoferum, a free-living nitrogen fixer. The results showed that Endosulfan could be adsorbed to the cell membrane and bind nonspecifically to proteins. A small portion of the adsorbed material could be transported to the cytosol. Endosulfan did not arrest growth, but instead promoted the development of cyst-like structures from the outer membrane.

Author: Buff, Klaus, Mano, Denise M.S., Langenbach, Tomaz
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
Physiological aspects, Environmental aspects, Pesticides, Nitrogen-fixing microorganisms

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Mode of action of Linenscin OC2 against Listeria innocua

Article Abstract:

Research was conducted to examine the effects of linenscin OC2 on the permeability characteristics of the cytoplasmic membrane of Listeria innocua and on different bioenergetic parameters. It was observed that linenscin OC2 induced a loss of intracellular K+, hydrolysis of internal ATP, depolarization of the cytoplasmic membrane, efflux of inorganic phosphate and stimulation and inhibition of the respiratory activity. Results provide evidence that the cytoplasmic membrane is the major target for linenscin OC2.

Author: Simonet, Jean-Marc, Boucabeille, Catherine, Letellier, Lucienne, Henckes, Gilles
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Permeability, Listeria

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Characterization of a novel plasma membrane protein, expressed in the midgut epithelia pf Bombyx mori, that binds to Cry1A toxins

Article Abstract:

The characterization of a novel 252-kDa protein (P252), isolated from brush border membranes of Bombyx mori, is described and it is shown that like the 120-kDa aminopeptidase N (APN), it can bind to all three Cry1A toxins. The properties of P252 are discussed in the context of the insecticidal mechanism of Cry toxins.

Author: Hossain, Delwar M., Shitomi, Yasuyuki, Moriyama, Kenta, Higuchi, Masahiro, Hayakawa, Tohru, Hori, Hidetaka, Sato, Ryoichi, Mitsui, Toshiaki
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
Science & research, Bacterial toxins, Properties

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Subjects list: Research, Cell membranes
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