[Obtaining human recombinant (serine-17) beta-interferon by the method of oligonucleotide-directed mutagenesis and its expression in Escherichia coli]. / Poluchenie rekombinantnogo (serin-17) beta-interferona cheloveka metodom oligonukleotidnapravlennogo mutageneza i ego ékspresiia v Escherichia coli.

The gene of human mutant (serine-17) fibroblast interferon was isolated with the use of highly efficient oligonucleotide-directed mutagenesis. On the basis of the constructed expression plasmid pPR-IFN Ser17 a strain producing human mutant beta-interferon (VKPM V-4678) was developed. It was shown that the specific activity of the human mutant (serine-17) fibroblast interferon was 1 order of magnitude higher than that of the recombinant interferon which reaches the specific activity of natural fibroblast interferon.

[MHC restriction of the anti-allotypic response of T-lymphocytes in vitro]. / MHC-restriktsiia antiallotipicheskogo otveta T-limfotsitov in vitro.

In vitro MHC restriction of antigen-specific T-cell proliferation to Igk-Ib allotype of Igk chain has been studied in inbred August rats, using polyclonal and monoclonal antibodies to RT-1 molecules. Igk-1b-specific proliferation of immune T cells was completely abrogated by alloantiserum specific for RT-1c (August) molecules. Monoclonal antibodies (MAb) to RT-1B ("1-A-like") molecules inhibited markedly the response (about 70-80% inhibition), while anti-RT-ID ("I-E-like") MAb caused but weak inhibition (about 25%). Thus, the data obtained demonstrate RT-1Bc molecule as a main restriction element of Igk-1b-specific T-cell response.

[Comparative analysis of the specificity of poly- and monoclonal antiallotypic antibodies and allotype-recognizing T-lymphocytes in rats]. / Sravnitel'nyi analiz spetsifichnosti poli- i monoklonal'nykh antiallotipicheskikh antitel i allotipraspoznaiushchikh T-limfotsitov krys.

Using concurrent solid-phase radioimmunoassay, it has been shown that rat immunoglobulin k chain, Igk-lb allotype, is represented by a single serologically defined determinant. Anti-Igk-lb T cells do not recognize this determinant and poly- and monoclonal anti-Igk-lb antibodies show no influence on Igk-lb-specific proliferative T-cell response in vitro to IgG (Igk-lb)-pulsed splenic antigen-presenting cells. It is suggested that T cells recognize allotypic determinant(s) of processed Ig (Igk-lb) molecule.

[Ir-gene control of rat T-lymphocyte proliferation in response to Ig allotype]. / Ir-gennyi kontrol' proliferatsii T-limfotsitov krys na allotip Ig.

Antigen-induced T-cell proliferation in vitro was adapted to the estimation of antiallotypic response to Igk-Ib immunoglobulin k chain allotype of MSU/b and Fisher rats in WAG, August and FI (WAG X August) rats. August and FI rat T lymphocytes responded to Igk-Ib alloantigen with stimulation indexes (SI) 3.8-5.0 (high responders), while WAG rat T lymphocytes showed practically no response (SI 0.9-1.8--low responders). These results correlate well with our previous findings of Ir-gene-controlled antiallotypic in vitro reactions in these rat strains. Effective antigen presentation to FI anti-Igk-Ib T cells was observed only using Igk-Ib-pulsed antigen-presenting cells (APC) of August responders, but not of WAG non-responders. FI T cells responded well to PPD-pulsed APC of both rat strains. The data confirm Ir-Igk-Ib-gene control and, therefore, MHC-restriction of antiallotypic response in inbred rats.

[Heart valve fibroblast Fc receptor study and the search for similar receptors in other tissues]. / Izuchenie Fc-retseptorov fibroblastov klapanov serdtsa i poiski podobnykh retseptorov v drugikh tknaiakh.

The data are confirmed about the presence of Fc-receptors reacting with human and rabbit IgG on the fibroblasts of human and bovine heart valves. It is shown the similar receptors are present on the fibroblasts of joints and L-cells. The receptors react largely with monomeric IgG. Clear-cut distinctions are revealed between the fibroblasts of heart valves and those of the myocardium which like other cells of myocardial interstitial connective tissue do not contain Fc-receptors.

[Interrelationship between the structure of IGG and its FC-fragment and their ability to react with protein A of Staphylococcus aureus]. / Vzaimosviaz' mezhdu strukturoi IGG i ego FC-fragmenta i ikh sposobnost'iu vzaimodeistvovat' s belkom A Staphylococcus aureus.

7S monomeric form of rabbit IgG, their dimers, IgG with the reduced interheavychain disulfide bond and proteolytic cleaved fragments from rabbit IgG were tested by hemagglutination inhibition test for their ability to bind staphylococcal protein A (SPA). SPA was found to combine with monomers of IgG and their papain Fc fragment. Facb, F(ab')2, Fab and pFc' fragments failed to react with SPA. At molar level Fc fragment retained 15% of IgG binding activity of SPA. After cleavage of the interheavychain disulfide bond of the IgG molecule its ability to react with SPA decreased 3-fold. As a result of spontaneous dimerization the IgG binding activity of SPA increased twelve-fold. The evidence obtained suggests an interrelationship between the IgG Fc fragment structure and its ability to interact with protein A is discussed.