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At least 685 records · Page 38Linked to original sources
PubMed1979

L-alanine--an essential amino acid for growth of lymphocytes in vitro.

A factor an ultrafiltrated (UM 10) extracts of calf thymus, liver and spleen stimulated the uptake of 3H-thymidine in DNA of cultured lymphocytes. The factor was purified by ion-exchange chromatography and gel chromatography and identified as alanine, which is lacking in the culture medium, RPMI 1640. An optimal amount of L-alanine increased the uptake of 3H-thymidine in DNA of lymphocytes from different species by about 100%. L-alanine should be regarded as a growth factor for lymphocytes in vitro and should be added to RPMI 1640, when this tissue culture medium is used for lymphocytes.

Alanine↗
PubMed1979

Further studies on splenic material inhibiting the growth of lymphocytes in vitro.

A material inhibiting growth of lymphocytes from different lymphoid organs and from different species was purified from calf spleen. A factor with a molecular weight of about 45,000 dal (estimated by gel chromatography) inhibited DNA synthesis and mitosis irreversibly in thymocytes and caused degenerative changes in the nucleus and the cytoplasm of the thymocytes as judged by electron microscopy. However, no decrease in cell number and no increase in dye uptake in a dye exclusion test were found. Growth inhibition was also demonstrated for human melanoma cells, but not for rat liver cells. The cytotoxicity and the lack of absolute lymphocyte specificity of the factor speak against its character as a lymphocyte chalone. A probably identical factor was purified from calf liver, but was not found in extracts of calf thymus.

Animals↗
PubMed1990

[The effect of vilozen on the immune status of bronchial asthma patients].

An immunological study of 163 patients with different forms of bronchial asthma revealed a distinct disturbance of the cellular link of immunity in these patients. Vilosen (a native non-protein immunomodulator extracted from the thymus of animals) possessing a prevailing action on T-cells was used for correction of the immune disorders. It was found that vilosen proved effective in the complex treatment of patients with atopic associated forms of bronchial asthma.

Adjuvants, Immunologic↗
PubMedDate not supplied

Ultrastructural modifications in mice spleen after "Imunotim' treatment.

Imunotim, a polypeptidic extract from bovine thymus, induces the appearance of barrier cells in the spleen; these cells form a syncytial network and play an important role in blood cleaning. They are of fibroblastic origin. The cytoplasm of the cells in the network is dense and contains vesicles that seem to be detached from the nucleolemma. The nuclei are of small sizes. Cells (maybe lymphocytes) in different stages of disintegration can be seen in the network.

Animals↗
PubMed1993

[Effect of thymic factor D on lipid peroxide, glutathione, and membrane fluidity in liver of aged rats].

The effects of thymic factor D (TFD) on aging were investigated in male Wistar rats at the age of 24 months. Thymic factor, polypeptides extracted from swine thymus, was given to aged rats in the dose of 2 mg.kg-1 sc every other day for 3 months. It was shown that TFU decreased the content of malondialdehyde (MDA) and lipofuscin in the liver of aged rats, accompanied by an increase of glutathione (GSH). Besides, the declined fluidity of hepatic mitochondrial and microsomal membranes in aged rats was recovered to the level of young adult rats by administration of TFD. It is suggested that TFD may possess beneficial effects on retarding the senile metabolic changes in hepatic cells.

Aging↗
PubMedDate not supplied

[Role of the vagus nerves in regulating the activity of the pentosephosphate carbohydrate metabolic pathway in the thymus and mesenteric lymph nodes].

Activity of key enzymes of pentosephosphate pathway glucose-6-phosphate dehydrogenase (G6PD) and transketolase was similar in extracts of thymus and mesenteric lymphatic ganglia. Within four weeks after dissection of vagus nerve at the level of thyroid gland the specific activity of G6PD and the total activity of the enzymes metabolizing ribose-5-phosphate were not altered in the tissue studied. The transketolase activity was inhibited in thymus tissue and lymphoid cells after right-side vagotomy. The pH-dependence of the transketolase reaction was studied in thymus extracts. After vagotomy the enzymatic activity was lower at all the pH values as compared with controls; the enzyme optimum activity was found at pH 7.5-7.8.

Animals↗
PubMedDate not supplied

The effect of some thymic extracts on antibody formation in rats and mice.

The influence of some thymic extracts TP1 and TP2 on the number of hemolytic plaque-forming cells (PFC) in the mouse spleen, on the titre of serum antibodies, S-typhy antiflagelar agglutinins and anti-influenza antibodies, was investigated. The results have shown that the hemolytic plaque-forming cells in the mouse spleen increase significantly, 2.3 times under the influence of the TP2 thymic extract in RAP mice inoculated with sheep red cells. In Wistar rats, inoculated with a formol-inactivated suspension of S. typhy and treated with TP2, the antibody titre increases 3.3 times at most. The increase is in relation to the dose of extract and the thymus batch from which the extract was prepared. TP1 also stimulates serum antibody formation in Wistar rats inoculated with A2 influenza vaccine. The antiinfluenza antibody titre increases 2.7 times under the influence of the thymic extract. The results also depend on the dose of extract and the thymus batch. In irradiated animals, the thymic extract had a protective effect. X-ray exposure of Wistar rats caused a 2.5 times decrease in the antiinfluenza antibodies titre. Under the influence of the TP1 thymus extract, the antibody titre increases 2.9 times as against the irradiated controls.

Animals↗
PubMed1977

Biochemical characterization of alkaline phosphatase in guinea pig thymus.

1. Alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) in guinea pig thymus was extracted optimally in 10 mM Tris - HCl buffer at pH 8.0 containing 5 g/l Triton X-100. 2. alpha-Glycerophosphate, beta-glycerophosphate and phenolphthalein monophosphate were hydrolyzed by thymus extract with a pH optimum at 9.8-10.0, whereas p-nitrophenylphosphate and alpha-naphthylphosphate were hydrolyzed with pH optima at 10.7-10.8 and beta-naphthylphosphate at pH 11.2. P-Nitrophenylphosphate and phenolphthalein monophosphate proved to be the most suitable substrates. 3. Alkaline phosphatase was effectively inhibited by EDTA, Zn2+, histidine and urea therefore resembling the inhibition characteristics of alkaline phosphatase in the placenta and kidney, but not that in the liver and intestine, which differed markedly. 4. DEAE-cellulose chromatography and polyacrylamide disc electrophoresis revealed three enzyme peaks which did not differ in their substrate specificities and modifier characteristics. 5. Polyacrylamide disc electrophoresis of thymus, serum, placenta, kidney, liver, bone and intestine revealed no alkaline phosphatase bands definitely unique to thymus.

Alkaline Phosphatase↗
PubMed1991

Extraction and differentiation of the Su autoantigen from calf thymus nuclei.

Antibodies to Su antigen have been reported previously as a distinct antigen-antibody system associated with connective tissue diseases; most specifically systemic lupus erythematosus and undifferentiated connective tissue disease. The Su antigen was first identified by double immunodiffusion using calf thymus nuclear extract (CTNE) as a source for Su antigen. In this report, enhanced extraction of Su antigen was achieved using deoxyribonuclease I (DNase) for preparation of CTNE. Only the Sm antigen was found in comparable quantities in the DNase CTNE. Western immunoblotting and immunoprecipitation employing DNase CTNE and extracts of [35S]methionine-labeled HeLa cells respectively were used for further characterization and differentiation of the Su antigen. Sera from patients positive for Su antibodies by double immunodiffusion were found to react most specifically with antigen components in a molecular weight range of approximately 50-55 kDa. These methods should assist in further understanding the biochemical properties of the Su antigen.

Ammonium Sulfate↗
PubMed1984

Comparison of various preparations of nuclear antigens by hemagglutination inhibition (HAI).

A clinical laboratory carrying out tests for antinuclear antibodies requires an efficient, reliable preparation method to produce a high yield of nuclear antigens at low cost and a very sensitive, specific assay method for antigen activity. Various tissues were employed for preparation of small nuclear ribonucleoprotein (snRNP) and Sm antigens for these purposes. Fresh calf thymus cells and nuclei, commercially available calf and rabbit thymus acetone powders, fresh rat kidney and liver cells were used as sources of antigens prepared similarly by methods published previously. Preparations of antigens from whole calf thymus cell extracts were prepared with and without inhibitors to protease and RNase. snRNP and Sm antigens were assayed at each preparation step by hemagglutination inhibition (HAI). Using HAI it was possible to routinely assay snRNP and Sm at nanogram/ml quantities which was 10(6) fold more sensitive than Ouchterlony immunodiffusion. Results were expressed as relative specific activity as compared with calf thymus nuclear extract prepared by conventional methods. Protease and RNase inhibitors did not significantly increase yields. Thymus was the best source of snRNP and Sm. Fresh calf thymus extract produced a good, stable, reliable quantity of antigens, whereas calf and rabbit thymus acetone powders provided antigen at higher specific activity with less labor but slightly lower yields. Thus, considering the total cost of preparations, commercial sources may be superior to fresh sources in the clinical laboratory setting. These studies also revealed the utility of the sensitive HAI test not only in the clinical laboratory but also for further research endeavors.

Animals↗