[Role of tumor necrosis factor in immunopathogenesis of pulmonary tuberculosis].

The activity of TNF-alpha in the serum was determined with ELISA basing on 2 monoclonal antibodies varying by epitopic specificity in 25 patients with pulmonary tuberculosis and 4 patients with chronic nonspecific respiratory diseases. TNF-alpha varied with tuberculosis severity and prognostic factors. Its level appeared the highest in fibrocavernous tuberculosis (405.

[Synthesis of tumor necrosis factor-alpha (TNF-alpha) by human monocytes in vitro].

The presence of TNF-alpha mRNA and protein in circulating human blood monocytes isolated by continuous Percoll gradient fractionation was studied. The technique of RNA isolation from the blood samples was used to study TNF-alpha mRNA expression. It was shown that human blood monocytes of healthy donors contained no presynthesized pool of TNF-alpha mRNA as well as no TNF-alpha protein.

[Localization of an antigenic determinant of recombinant interleukin-2, recognized by monoclonal antibody 13B1].

We suggest a simple approach to localization of antigenic determinants for the monoclonal antibody 13B1 raised against recombinant human interleukin-2. The approach is based on the limited trypsin proteolysis, peptide separation by the O'Farrell method and identification of the peptides, interacting with monoclonal antibodies, and comparison of the charge and length of these peptides with the corresponding values of theoretically possible peptides.

[Monoclonal antibodies to an artificial immunogen, specifically demonstrating phosphotyrosine-containing proteins].

The importance of protein phosphorylation at tyrosyl hydroxy groups in the control of cell proliferation has recently been established. For identification of tyrosine-phosphorylated proteins, monoclonal antibodies (Mabs) against artificial immunogens containing O-phosphotyrosine (pTyr) or tripeptide pTyr-Gly-Gly as haptens were generated; the haptens were coupled to carrier proteins (bovine serum albumin, human immunoglobulin, keyhole limpet hemocyanin). After immunization of mice with pTyr coupled to keyhole limpet hemocyanin, Mabs were generated which were highly specific for pTyr and did not cross-react with O-phosphoserine, O-phosphothreonine, tyrosine or nucleoside-5'-monophosphates.