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Results for “Fenthion”

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PubMed1992

Scientific discourse, in public.

The experience of writing for a wider audience has benefits and drawbacks. Attempting to make scientific issues more accessible to non-scientists is no easier than explaining them to peers. Indeed, explaining toxicological data such as solvent measurements from a hazardous waste site can be even more difficult, especially in addressing those living next to the site. Alastair Hay reconsiders his experience in two cases that brought toxicology under public scrutiny.

Chemical Industry↗
PubMed1988

Selected neurotoxins.

The small animal practitioner is faced with an infinite number of potential toxins in our modern environment. Unapproved usage of drugs and insecticides requires the practitioner to keep informed about the development of new toxic syndromes. Recreational drug toxicosis in animals is still seen with some frequency in clinical practice and should not be overlooked, even when the owner denies the possible exposure. In this article, we have discussed a few of the more common and newer neurotoxicities seen in clinical practice today. Neurologic toxicities are complex, but treatment can be rewarding if early diagnosis is made and aggressive therapy is instituted. The practitioner will find it worthwhile to establish contact with a toxicologist or poison information center for additional support when necessary.

Animals↗
PubMed1995

The Pto bacterial resistance gene and the Fen insecticide sensitivity gene encode functional protein kinases with serine/threonine specificity.

The catalytic activity and amino acid specificity of the tomato Pto and Fen kinases were investigated. The Pto and Fen genes were fused to the carboxyl terminus of the maltose-binding protein and expressed in Escherichia coli. Incubation of the purified fusion proteins with [gamma-32P]ATP in an in vitro assay showed that both proteins were capable of autophosphorylation. Mutant fusion proteins in which the conserved lysine residue of subdomain II was changed to a glutamine were unable to autophosphorylate. Phosphoamino analysis of the active fusion proteins indicated that both kinases phosphorylate serine and threonine residues but not tyrosine.

Amino Acid Sequence↗