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1.
Bioorg Khim ; 30(2): 201-7, 2004.
Article in Russian | MEDLINE | ID: mdl-15143677

ABSTRACT

A method of the competitive immunochromatographic assay of the pesticides 2,4-D (2,4-dichlorophenoxyacetic acid) and simazine (2-chloro-4,6-bis(N-ethylamino)-1,2,5-triazine) in aqueous samples was developed. Monoclonal antibodies to these pesticides labeled with colloidal gold were used to visualize the results. The sensitivity of the 2,4-D and simazine assay is 12 ng/ml, and the time of analysis is 3-7 min. The method does not differ in sensitivity from the competitive EIA using conjugates of monoclonal antibodies to the pesticides with horseradish peroxidase; however, the time of the EIA is 1.5 h. The immunochromatographic method of the pesticide detection is available and simple and may be recommended for the development of assays of any other low-molecular compounds. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 2; see also http://www.maik.ru.


Subject(s)
2,4-Dichlorophenoxyacetic Acid/analysis , Antibodies, Monoclonal/immunology , Chromatography/methods , Gold Colloid/chemistry , Simazine/analysis , 2,4-Dichlorophenoxyacetic Acid/immunology , Immunoenzyme Techniques , Sensitivity and Specificity , Simazine/immunology
2.
Bioorg Khim ; 26(3): 231-7, 2000 Mar.
Article in Russian | MEDLINE | ID: mdl-10816822

ABSTRACT

Detecting labels based on water dispersions of colloidal textile dyes were developed that are useful in various analytical and diagnostic test systems for a simple visual assessment of the assay. Colored water-insoluble particles of dyes were used for the sorptional immobilization of streptavidin on their surface. The resulting streptavidin-dye (STR-DYE) complexes possessed a high visualizing capacity and were used for the combined detection of pesticides (simazine and 2,4-dichlorophenoxyacetic acid) by noninstrumental immunoassay (DYE-comb-assay, competitive dot-immunoassay in the comb format). The detection limits and the duration of our DYE-comb-assay (4 ng/ml, 20-25 min), HRP-comb-assay (competitive dot-immunoassay in the comb format using the enzymic conjugate of STR with horseradish peroxidase) (16 ng/ml), and the traditional competitive ELISA (12-16 ng/ml, 1.5 h) were compared. This DYE-comb-assay is simple enough and can be used under field conditions.


Subject(s)
2,4-Dichlorophenoxyacetic Acid/analysis , Colloids , Immunoassay/methods , Simazine/analysis , 2,4-Dichlorophenoxyacetic Acid/immunology , Sensitivity and Specificity , Simazine/immunology
3.
Bioorg Khim ; 13(1): 20-6, 1987 01.
Article in Russian | MEDLINE | ID: mdl-3032208

ABSTRACT

The nucleotide sequence of the cDNA, containing coding region of the alpha-subunit of the pig kidney Na+, K+-ATPase, was determined. The region contains 3063 b.p. coding for 1021 amino acid residues. In the course of processing, five amino acid residues are cleaved to yield the mature Na+, K+-ATPase alpha-subunit containing 1016 amino acid residues.


Subject(s)
Genes , Kidney/enzymology , Sodium-Potassium-Exchanging ATPase/genetics , Amino Acid Sequence , Animals , Base Sequence , Swine
4.
Nucleic Acids Res ; 10(13): 4035-44, 1982 Jul 10.
Article in English | MEDLINE | ID: mdl-6287430

ABSTRACT

The primary structure of the E. coli rpoC gene (5321 base pairs) coding the beta'-subunit of RNA polymerase as well as its adjacent segment have been determined. The structure analysis of the peptides obtained by cleavage of the protein with cyanogen bromide and trypsin has confirmed the amino acid sequence of the beta'-subunit deduced from the nucleotide sequence analysis. The beta'-subunit of E. coli RNA polymerase contains 1407 amino acid residues. Its translation is initiated by codon GUG and terminated by codon TAA. It has been detected that the sequence following the terminating codon is strikingly homologous to known sequences of rho-independent terminators.


Subject(s)
DNA-Directed RNA Polymerases/genetics , Escherichia coli/enzymology , Genes , Amino Acid Sequence , Base Sequence , Codon/genetics , DNA Restriction Enzymes , Escherichia coli/genetics , Macromolecular Substances , Operon , Protein Biosynthesis
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