Publications by authors named "V V Basevich"

Triethylaluminum Al(CH), TEA, and triethylborane, B(CH), TEB, are transparent, colorless, pyrophoric liquids with boiling points of approximately 190 °C and 95 °C, respectively. Upon contact with ambient air, TEA, TEB, as well as their mixtures and solutions, in hydrocarbon solvents, ignite. They can also violently react with water.

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To find out the mechanism of ceruloplasmin (CP) oxidase activity CP interaction with organic substrates adrenaline (AD), catechol, p-phenylenediamine) and Fe2+ was investigated. CP was shown to interact with the above substrates according to the Theorell-Chance mechanism to form a kinetically insignificant ternary complex. The oxygen molecule binds first to CP followed by the molecule of electron donor: the inhibition of enzymatic oxidation by the reaction product is competitive.

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In order to elucidate the protective effect of human ceruloplasmin (CP) on erythrocytes in patients with hepatocerebral dystrophy (HCD), the parameters reflecting the interaction of CP from the blood of healthy donors (n-CP) and of HCD patients (h-CP) with erythrocytes from healthy donors (n-ER) and from HCD patients (h-ER) were estimated. The protective effects of n-CP and h-CP on n-ER and h-ER during the Cu2+-induced lysis were compared. It was shown that the ability of h-CP to prevent the human ER breakdown upon Cu2+-induced lysis is much lower (approximately 3-fold) than that of n-CP.

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Ceruloplasmin (CP) preparations have been used as the reference agents in transition of this protein oxidase activity to blood serum concentrations; the mean concentrations of serum CP varied from 175 to 310 mg/l, depending on the biochemical characteristics of the preparations. Adjustment by the blood serum copper level has proved adequate for clinical studies. CP activity has been found increased in some patients with disseminated sclerosis and lateral amyotrophic sclerosis.

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The structural fragments of the human ceruloplasmin (CP) molecule and of erythrocyte receptors which provide for the specific interaction of CP with erythrocytes were identified, and their properties were investigated. The interaction of CP with erythrocytes, both intact and treated with neuroaminidase and proteolytic enzymes (trypsin, chymotrypsin, papaine, pronase E) is described. Experiments with CP reception were performed at 4 degrees C, using [125I]CP and [125I]asialo-CP.

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