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Preparation of substituted methylarsonic and arsonoacetic acids

Article Abstract:

A reaction between alkaline arsenite and dichloroacetic acid yields arsonochloroacetic acid, decarboxylation of which, under standard conditions, produces chloromethylarsonic acid. Bromination of arsonoacetic acid results in dibromomethylarsenic acid through decarboxylation. The hindrance to a displacing nucleophile by one of the oxygen atoms in the -XO(sub 3)(super 2-) group that is positioned antiperiplanar to the halogen atom by the arsono or phosphono group makes the displacement of the halide difficult.

Author: Sparkes, Michael J., Dixon, Henry B.F.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Analysis, Arsenic compounds, Organic compounds, Chloroacetic acids, Organic compound synthesis

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Conservation of the amino-terminal epitope of elongation factor Tu in eubacteria and archaea

Article Abstract:

SPOTScan analysis of synthetic peptides, Western blot analysis of purified elongation factor Tu (EF-Tu) domains and site-directed mutagenesis studies were used to localize the conserved epitope within the EF-Tu molecule and to examine its sequence. Western blot analysis of the 1-3 terminus of hermus thermophilus indicated that the epitope was located at the N terminus. Site-directed mutagenesis of the EF-Tu domain one of Mycoplasma hominis confirmed the location of the epitope.

Author: Baensch, Melanie, Frank, Ronald, Kohl, Jorg
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
Mutagenesis, Antigenic determinants

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Molecular analysis of Physarum haemagglutinin I: lack of a signal sequence, sulphur amino acids and post-translational modifications

Article Abstract:

Physarum polycephalum elucidates haemagglutinin I, a protein able to agglutinate erythrocytes. The coding DNA for this lectin has been identified and cloned. The predicted gene product is a 104 amino acid polypeptide with a molecular weight similar to the native protein indicating that there is no posttranslational modification on the translated polypeptide. The predicted primary structure of the haemagglutinin I is unique indicating that it is a novel lectin.

Author: Morita, Masashi
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
Genetic aspects, Lectins, Molds (Fungi), Agglutinins

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Subjects list: Research
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