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Carbonyl groups in plasma protein in children with malignant brain tumors

100%

Popadiuk S. , Korzon M. , Renke J. , Wozniak M.

Polish Journal of Environmental Studies

1998

tom 07

nr 6

Amount of soluble and carbonylated collagen in oxygen-damaged mink skin

75%

Riis B. , Lohi O.

Zeszyty Naukowe. Przegląd Hodowlany

1996

tom 29

Oxidative modification of ovalbumin

75%

Olszowski S. , Olszowska E. , Stelmaszynska T. , Krawczyk A. , Marcinkiewicz J. , Baczek N.

Acta Biochimica Polonica

1996

tom 43

nr 4

Stimulated neutrophils (PMNL) are a source of the active oxygen species: O2, H2O2 and HOCl/OCT which in turn can act on proteins yielding a variety of mixed oxidation products. A system is proposed in which a model protein — ovalbumin (OVA) first undergoes chlorination by HOC1/OCT and next is oxidised by H2O2. The modification of functional groups (-NH2, -SH, -S-S-, >C=0, Tyr and Trp) in OVA was monitored as well as their accessibility to promote aggregation. Chlorination resulted in additional inter- or intra -S-S- bond formation followed by a decrease in the total sulfhydryl group content. Amino groups were oxidised to carbonyl moieties with a concomitant acidic shift of pi. Formation of chlorotyrosine at the chlorination step was confirmed and its further H202-mediated transformation to bityrosine was demonstrated. It has also been confirmed that tryptophan, and not tyrosine, is the first target for chlorination. SDS/PAGE and HPLC profiles revealed that HOCiyOCl" chlorination promotes formation of aggregates stabilised by non covalent bonds. In conclusion, we suggest that a dramatic change in the OVA molecule structure begins when the molar excess of HOC1/OC1 is about 2 per one reactive group in OVA.

Air oxidation of potato starch over zinc (II) catalyst

63%

Gumul D. , Gambus H. , Gibinski M.

Electronic Journal of Polish Agricultural Universities. Series Food Science and Technology

2005

tom 08

nr 4

Nowe poglądy na rolę bioflawonoidów

51%

Bogdanska H.

nr 1

Surface properties of polyethylene pre-treated by low-temperature plasma

51%

Novak I. , Popelka A. , Sedliacik J. , Valentin M. , Chodak I. , Kleinova A. , Vanko V. , Preto J.

Annals of Warsaw University of Life Sciences - SGGW. Forestry and Wood Technology

2012

tom 79

The protective effects of selenoorganic compounds against peroxynitrite-induced changes in plasma proteins and lipids

51%

Nowak P. , Saluk-Juszczak J. , Olas B. , Kolodziejczyk J. , Wachowicz B.

Cellular and Molecular Biology Letters

2006

tom 11

nr 1

Many selenoorganic compounds play an important role in biochemical processes and act as antioxidants, enzyme inhibitors or drugs. The effects of a new selenocompound — bis(2-aminophenyl)-diselenide on oxidative/nitrative changes in human plasma proteins induced by peroxynitrite (ONOO−) were studied in vitro and compared with the those of ebselen, a well-known antioxidant. We also studied the role of the tested selenocompounds in peroxynitrite-induced plasma lipid peroxidation. Exposure of the plasma to peroxynitrite (0.1 mM) resulted in an increase in the level of carbonyl groups and nitrotyrosine residues in plasma proteins (estimated using the ELISA method and Western blot analysis). In the presence of different concentrations (0.025–0.1 mM) of the tested selenocompounds, 0.1 mM peroxynitrite caused a distinct decrease in the level of carbonyl group formation and tyrosine nitration in plasma proteins. Moreover, these selenocompounds also inhibited plasma lipid peroxidation induced by ONOO−1 (0.1 mM). The obtained results indicate that in vitro bis(2-aminophenyl)-diselenide and ebselen have very similar protective effects against peroxynitrite-induced oxidative/nitrative damage to human plasma proteins and lipids.

Ochronny wplyw N-acetylocysteiny na prooksydacyjne i proapoptotyczne dzialanie tiuramu w komorkach V79 chomika chinskiego

44%

Kurpios-Piec D. , Grosicka-Maciag E. , Czeczot H. , Szumilo M. , Grzela T. , Rahden-Staron I.

Bromatologia i Chemia Toksykologiczna

2010

tom 43

nr 3

354-361