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6.
Article in Russian | MEDLINE | ID: mdl-7660713

ABSTRACT

In the approbation of the enzyme-linked immunosorbent assay (ELISA) system on the basis of F(ab)2 fragments of antistaphylococcal antibodies on 307 cultures of the representatives of the genera Staphylococcus, Pseudomonas and Proteus high sensitivity, specificity and effectiveness of ELISA for the quantitative and qualitative evaluation of the alpha-hemolytic activity of S.aureus were established. The ELISA system has made it possible to additionally detect alpha-hemolysin in 62% of S.aureus strains classified with as nontoxigenic strains using hemolysis test in Petri dishes. The sensitivity limit of this method is 0.0005 binding units or 1.0 ng in terms of protein content. The use of the ELISA system may be recommended for the study of the toxigenic properties of staphylococci.


Subject(s)
Antibodies, Bacterial/immunology , Bacterial Toxins/analysis , Hemolysin Proteins/analysis , Immunoenzyme Techniques , Immunoglobulin Fab Fragments/immunology , Staphylococcus aureus/immunology , Analysis of Variance , Antibody Specificity , Evaluation Studies as Topic , Humans , Immunoenzyme Techniques/statistics & numerical data , Proteus/immunology , Pseudomonas/immunology , Sensitivity and Specificity , Spectrophotometry , Time Factors
7.
Article in Russian | MEDLINE | ID: mdl-3687296

ABSTRACT

An enzyme immunoassay system for the detection of diphtheria toxin and the products of its degradation has been developed on the basis of the enzyme-linked immunosorbent assay. To sensitize the assay plates, bivalent F(ab)2-fragments of purified antidiphtheria antibodies at a concentration of 10.0 micrograms/ml, obtained from the blood serum of hyperimmunized rabbits, have been used. Specific conjugates have been prepared with the use of F(ab)2-fragments of purified antidiphtheria antibodies obtained from the blood serum of hyperimmunized horses. The optimum time and temperature conditions of the assay have been established. The new enzyme immunoassay system permits the detection of diphtheria toxin and the products of its degradation in biological substrates at a concentration of 10.0-5.0 ng/ml.


Subject(s)
Diphtheria Toxin/analysis , Diphtheria Toxoid/analysis , Enzyme-Linked Immunosorbent Assay , Animals , Enzyme-Linked Immunosorbent Assay/instrumentation , Evaluation Studies as Topic , Humans , Hydrogen-Ion Concentration , Immunoglobulin Fab Fragments/immunology , Indicators and Reagents , Rabbits , Temperature , Time Factors
8.
Zh Mikrobiol Epidemiol Immunobiol ; (4): 114-5, 1982 Apr.
Article in Russian | MEDLINE | ID: mdl-7080755

ABSTRACT

The treatment of experimental tetanus intoxication in 120 rabbits by the intrathecal injection of antitoxins revealed that the therapeutic effect was directly proportional to the dose of antitoxins, expressed in antitoxic units. The maximum effect (the survival rate 78.6%) was obtained by the injection of antitoxins purified on immunoadsorbents and containing no admixtures. The use of such antitoxins ensured the absence of postinjection complications, while commercial antitetanus serum "Diaferm-3" gave only 16.7% survival rate and produced the equal percentage of postinjection complications.


Subject(s)
Tetanus Antitoxin/therapeutic use , Animals , Dose-Response Relationship, Immunologic , Drug Evaluation, Preclinical , Female , Immunochemistry , Male , Rabbits , Tetanus/therapy , Tetanus Antitoxin/administration & dosage , Tetanus Antitoxin/isolation & purification , Time Factors
9.
Vopr Med Khim ; 24(5): 608-12, 1978.
Article in Russian | MEDLINE | ID: mdl-706252

ABSTRACT

A modified method is described for isolation of acetylcholinesterase from human erythrocytes using an additional step of gel filtration on Sephadex G-75. Preparations of acetylcholinesterase were liberated from thromaboplastic activity and their specific activity was increased due to removal of low molecular proteins and of the products of destruction of hemoglobin. Content of A and B isoantigens in the preparations obtained was rather low and content of hemoglobin, combined with other proteins in the form of oxyhemoglobin, did not exceed 12% of the total protein.


Subject(s)
Acetylcholinesterase/isolation & purification , Erythrocytes/enzymology , Chromatography, Gel , Humans
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