[Cysteine proteinases and their inhibitors in the development of mouse HA-1 hepatoma and antineoplastic therapy]. / Tsisteinovye proteinazy i ikh ingibitory pri razvitii myshinoi HA-1 gepatomy i protivoopukholevoi terapii.

Development of murine HA-1 hepatoma was accompanied by increased activity of cathepsin B (in ascitic cells), cathepsin D (in ascitic fluid) and increased activity of procathepsin B. There were some changes of cysteine proteinases in liver and spleen, not involved directly into tumor growth. The most prominent changes included the decreased level of cysteine proteinase inhibitors cystatin C and stefin A in ascitic cells (and to a lesser degree in liver tissue). During tumor development serum cystatin C concentration decreased by 3-times compared to intact mice. Treatment by antitumor drug Ukraine increased life span of mice with HA-1 hepatoma (transplanted intravenously), decreased the increment of tumor weight. In ascite such treatment caused a decrease of number of tumor cells and an increase of number of macrophages. Ukraie (administered once or 5-times in a dose of 0.5 mg per mice) increased cystatin C level, revealing protective mechanism of action.

[Immunoenzyme technique for analysis of cystatin C in serum of patients with hemoblastosis]. / Immunofermentnyi analiz tsistatina C v syvorotke krovi bol'nykh gemoblastozami.

Cystatin C is a low-molecular endogenous inhibitor of cysteic proteinases. Sets for immune-enzyme assay of cystatin C in human blood serum (KRKK, Slovenia) were made used of in the case study. The concentration of cystatin C (CCC) in blood serum was found to be higher in cases of certain hemoblastoses (Non-Hodgkin's disease, lymphogranulomatosis and multiple myeloma), with the highest concentration of the inhibitor being observed in patients with resistance to the conducted polychemotherapy and a poor prognostication. The treatment of Non-Hodgkin's disease and of lymphogranulomatosis brought about a normalized CCC in blood serum. It was suggested that CCC in blood serum reflects a nature of tumor growth and, obviously, it can be a criterion in assessing the therapy efficiency. The concentration of alpha 1-proteinases inhibitor remained unchanged before and after treatment.

[Immunochemical homology of HIV-1 envelope proteins and human apolipoprotein AI]. / Immunokhimicheskoe sootvetstvie obolochechnykh belkov VICh-1 i apolipoproteina AI cheloveka.

Immunochemical homology of envelope HIV proteins and human apolipoprotein A-I was for the first time detected by ELISA. Immunochemical reactions between antibodies to apoA-I and HIV envelope proteins and between apoA-I and anti-HIV antibodies present in the blood of AIDS patients were shown. These data suggest that the homology of surface HIV proteins and human apoA-I can lead to competitive relationships impeding the involvement of human apoA-I in gene expression regulation.

[Effect of long-term cold exposure on apoprotein A-I, B, and E levels in the rat serum]. / Vliianie dlitel'nogo okhlazhdeniia na soderzhanie apoproteinov A-I, B i E v syvorotke krovi krys.

An increase in the quantity of triglyceride-rich VLDL as well as the total fraction VLDL and LDL occurred following the cold adaptation. The contents of apoB and apoE, respectively, increased. However, a 5-15-day exposure to cold decreased the LDL2 and apoA-1 content. In 49 days of the experiment, the LDL2 and apoA-1 content was restored.

Enzyme-linked immunosorbent assay for apolipoproteins A-I and B in the urine of patients with nephrotic syndrome. / Tverdofaznyi immunofermentnyi analiz apolipoproteinov A-I i B v moche liudei s nefroticheskim sindromom.

Enzyme-linked immunosorbent assay (ELISA) has been used for measuring apolipoproteins A-I and B in the urine. ApoB is absent in urine of healthy subjects, and apoA-I is determined in trace quantity. In patients with chronic glomerulonephritis quantity of apoA-I in urine was 117 times as much as in control group. ApoB is present in urine of patients in considerable quantity (1528 +/- 315 micrograms/l). The ELISA method for determining apoA-I and apoB in urine makes it possible to evaluate the gravity of pathological process in kidney.

[Synthesis of insulin fragments and study of their physicochemical and immunological properties]. / Sintez fragmentov insulina i izuchenie ikh fiziko-khimicheskikh i immunologicheskikh svoistv.

A two-chain peptide was predicted as a receptor binding site of insulin on the basis of theoretical conformational analysis. This dimeric peptide, consisting of the C-terminal A18-A21 tetrapeptide of the insulin A-chain and the C-terminal B17-B30 tetradecapeptide of the insulin B-chain connected with a disulfide bridge, was synthesized along with the C-terminal nonadecapeptide. The analysis of the aggregation state of human insulin and the synthesized linear and dimeric peptides was performed by the small-angle X-ray scattering method. Specific antibodies were produced after rabbit immunization with the dimeric peptide-BSA conjugate. The immunochemical identity of the model dimeric peptide and the corresponding fragment of the insulin molecule were shown by immunoenzyme analysis.

[Detection of apoprotein A-1 immunoreactivity in chromatin of rat hepatocytes]. / Obnaruzhenie apoprotein A-1-immunoreaktivnosti v khromatine iader gepatotsit krys.

The binding of 125I-labeled lipoproteins to subcellular structures of rat hepatocytes was studied. The protein component of HDL, LDL, and VLDL was found in large and small membranes, nuclei, mitochondria, lysosomes, microsomes, and cell cytosol. The presence in liver nuclear chromatin of proteins immunochemically related to apoA-1 was demonstrated by solid phase immunoenzymatic analysis, dot immunoanalysis, and immunoelectroblotting. The apoprotein A-1 immunoreactivity was detected in transcriptionally inactive total chromatin, transcriptionally active chromatin, and nuclear matrix. The specific apoA-1 immunoreactivity of transcriptionally active chromatin and nuclear matrix was two times as low as that of total and transcriptionally inactive chromatin. Immunoelectroblotting revealed two proteins possessing an apoA-1 immunoreactivity (M(r) 28 and 14 kDa). The 28 kDa protein was found in transcriptionally active chromatin and nuclear matrix, while the 14 kDa one--only in transcriptionally inactive chromatin. the roles of apoproteins in lipid transport to nuclei and the maintenance of chromatin in a transcriptionally active state are discussed.

[Determination of apoprotein B using the method of solid-phase immunoenzyme analysis]. / Opredelenie apoproteina B metodom tverdofaznogo immunofermentnogo analiza.

Indirect solid-phase enzyme immunoassay was used to measure apoB in human blood serum. ApoB obtained by traditional gel filtration in sepharose 4B and high-performance liquid chromatography was used as an antigen. Anti-apoB antibodies were immunochemically identified. Working regimens for the components and conjugates employed were selected. ApoB level in human blood serum, determined by this method, has made up 0.83 +/- 0.1 g/l in men and 0.88 +/- 0.1 g/l in women.

[Determination of apoprotein A-1 by immunoenzyme analysis]. / Opredelenie apoproteina A-1 metodom immunofermentnogo analiza.

Indirect solid-phase immunoenzymatic assay was improved and adapted for quantitative estimation of apo A-I in blood serum. Immunochemical identification of apo A-I was carried out and specific antibodies were obtained. Various procedures of blood serum pretreatment affected dissimilarly the detection of antigenic determinants in apo A-I. Presence of tetramethyl urea in blood serum increased by 30% the latent antigenic determinants accessibility.

[Solid-phase immunoenzyme analysis of apoprotein A-1]. / Tverdofaznyi immunofermentnyi analiz apoproteina A-1.

The authors have optimized indirect solid-phase enzyme immunoassay for measuring human blood serum apoA-1. Immunochemical identification of the obtained apoA-1 and specific antibodies has been carried out, working regimens for the components and conjugates employed have been selected. Relationship between the method of preliminary treatment of the serum and the completeness of detected apoA-1 antigenic determinants is demonstrated. Normal blood serum apoA-1 level is 1.06 +/- 0.1 g/l in females and 1.05 +/- 0.1 g/l in male subjects.