The precipitation of histone-proteins with trichloroacetic acid.
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Biomedical subjects
Publications and source records attributed to A Lakatos.
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A new histochemical reaction for the identification of histone type basic proteins has been developed. Carbonyldiimidazol is used to activate the basic proteins of TCA-extracted nuclei, their m-aminophenylboronic acid complex is prepared, and the DNA-free, histone-containing nuclei are stained with toluidine blue at pH 5.5.
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The epsilon amino groups of histone proteins were eliminated by condensation with glucose, fructose or mannose. The trichloroacetic acid extracted, DNA negative nuclei treated with reducing sugars, stained easily with basic dyes.
Earlier examinations have shown that reducing sugars mainly react with the epsilon-amino group of lysine. After DNA extraction, lysine-rich histone proteins of alcohol fixed nuclei of rat organs were treated with glucose-6-phosphate. It was possible to selectively stain the histone type proteins of DNA negative nuclei with basic dyes.
Five patients are reported in whom brownish grey discoloration occurred on the light-exposed parts of the dermis after long-term amiodarone-medication. Histological investigation shows that the deposition of lipofuscin in the small veins and perivasal superior part of the corium is responsible for the occurrence of this discoloration. With reference to recent data in the literature, the pathomechanism and prevention of this pigmentation are discussed.
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The serum antihistone antibody (AHA) positivity of patients with various autoimmune diseases was compared with their positive reaction for antinuclear factor, rheumatoid factor, lupus erythematosus factor, cryoglobulin, immunocomplex, C-reactive protein, total protein, gamma globulin, IgG and IgM. In non-drug-induced SLE cases the predictive value of the AHA test was not higher than that of the other tests. It was striking that in 42% of patients with non-autoimmune disease aged over 70 the AHA test was positive. Elevated IgM values were recorded in about 70% of positive AHA samples.
The kinetics of glycation of histone proteins was studied. The glucose uptake of H1 linker histone reached saturation attained after an exponential course. H2-H4 core histone and total histone exhibited two-phase courses differing in time. With the uptake of glucose, the electromobility of the fractions changed. The kinetic results are explained in terms of interaction between proteins.