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Magnetic transformation in Ni-Mn-In Heusler alloy

100%

Kuzma M. , Maziarz W. , Stefaniuk I.

tom Vol. 60, No. 3, part 1

435--438

Magnetic properties of a Ni50Mn35.5In14.5 Heusler ribbon were studied by ferromagnetic resonance (FMR) in the temperature range of 335–100 K. In the temperature region of 265–170 K, the FMR signal disappeared, in spite of the fact that this region comprised the main crystal transformation temperatures: Ms, Mf, As, Af. In the austenite crystal state, a weak antiferromagnetic interaction was observed, whereas ferromagnetism was detected in the low temperature martensitic state.

Wplyw zwiazkow fenolowych na transferazy glutationowe z mozgu ssakow

100%

Sawicki J. , Kuzma M. , Baranczyk-Kuzma A.

Bromatologia i Chemia Toksykologiczna

2001

tom 34

nr 2

149-154

W pracy badano wpływ fenolu i jego pochodnych (siarczan fenolu, 1-naftol, siarczan 1-naftolu, p-nitrofenol, siarczan p-nitrofenolu, p-nitroanizol, p-aminofenol, fenacetyna, paracetamol) na aktywność obojętnej izoformy transferazy glutationowej (GST) [EC 2.5.1.18] wyizolowanej z kory mózgu wołu i świni. Stwierdzono, że pochodne fenolu silniej hamują aktywność badanego enzymu niż sam fenol. Wrażliwość GST na działanie tych związków w mniejszym stopniu zależy od mózgowej lokalizacji enzymu niż od ich budowy chemicznej.

Phenol and 1-naphthol do not affect, or slightly decrease, the in vitro activity of the neutral forms of glutathione-5-transferase (GST) isolated from bovine and pig brain cortex. Phenol and naphthol sulfates are much stronger, competitive inhibitors of those enzymes. Among the studied chemicals, p-nitrophenol has the strongest GST-inhibiting effect and, like p-aminophenol, its reduced derivative, inhibits the enzyme non-competitively. Sulfation or methylation of the -OH group decreases the inhibiting effect of p-nitrophenol and changes the site of its binding to the enzyme. Acetylation of the amino group of p-aminophenol lowers the inhibitory effect of this compound; thus the phenacetin and paracetamol analgetics do not at all, or only slightly, inactivate brain glutathione-S-transferases. GST sensitivity to phenols depends on the chemical structure of the latter rather than on enzyme location in the brain.

Zmiany w ekspresji izoform bialka tau w mozgu myszy w zaleznosci od wieku

75%

Usarek E. , Kuzma M. , Kazmierczak B. , Muench C. , Ludolph A. C. , Baranczyk-Kuzma A.

tom 62

nr 02

231-233

au is a microtubule-associated protein important for the assembly and stabilization of microtubules. Six tau isoforms are produced in the central nervous system from one single gene as a result of the alternative splicing of exons 2, 3 (N-terminal part) and exon 10 (C-terminal part). The shortest isoform (2-3-10-, 0N 3R) is characteristic for fetal brains, whereas the remaining (2+3-10-, 1N 3R; 2+3+10-, 2N 3R; 2-3-10+, 0N 4R; 2+3-10+, 1N 4R; 2+3+10+, 2N 4R) for adult brains. The aim of the study was to establish a profile of tau protein variants in the C57BL/6J mouse frontal cortex during the aging process. The total RNA was isolated from tissues, followed by reverse transcription and PCR reaction. It was found that the sequence encoded by exon 10 was absent in the youngest 5-day old newborns (isoform 3R), while it was present in 21, 70 and 140-day old animals (isoform 4R). The most abundant isoform in 5-day old mice was 1N and accounted for 66% of the total tau protein. The percentage of 1N isoforms lowered with age and was 31% in 140-day old animals. The total percentage of 0N isoforms was 11% in 5-day old mice and was approximately threefold lower than in each of the older groups. It may be concluded that alternative splicing of the tau protein undergoes age-dependent regulation in the mouse brain cortex.

Does preconditioning protect against experimental ischaemia-reperfusion injury via cholinergic stimulation?

63%

Dzierzkowska J. , Gajewska J. , Witanowska A. , Deptuch T. W. , Kurenko M. , Gajewski M. , Mautiris J. , Kuzma M. , Dron T. , Maslinski S.

tom 48

nr 2