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1

The effect of semisynthetic derivatives of phenolic lipids on activity of membrane enzymes

100%
Czajkowska D., Stasiuk M., Kozubek A.
Cellular and Molecular Biology Letters
|
2005
|
tom 10
|
nr Suppl.
2

Determination of octanol-water partition coefficients for long-chain homologs of orcinol from cereal grains

100%
Kozubek A.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 2
Polycratic reversed-phase high-performance liquid chromatography (RPHPLC) was used for estimation of the octanol/water partition coefficient for three highly hydrophobic long chain orcinol homologs. The homologs studied (C 15:0, C 17:0 and C 19:0) showed high preference for hydrophobic phase as evidenced by their high octanol/water partition coefficient (log P o/w ) values of 7.02-7.74; 8.71-9.47 and 10.49-11.32 for the 95% prediction interval, respectively. Experimentally estimated values were compared with log P values calculated with the use of several fragmental systems. The experimental values of log P o/w are in best agreement to those calculated with the use of the Klopman system (Klopman, Gv Namboodiri, K. & Schochet, M., 1985, /. Comput. Chem. 6,28-38). The lack of appropriate standard compounds with known log P 0/w in the range over 6 markedly affected the accuracy of experimental determinations.
3

Studies of the amhiphilic properties of MSAR

100%
Stasiuk M., Kociubinska A., Gubernator J., Cieslik K., Kozubek A.
Cellular and Molecular Biology Letters
|
2002
|
tom 07
|
nr Suppl.
4

Inhibition of soybean lipoxygenases by resorcinolic lipids from cereal bran

72%
Deszcz L., Kozubek A.
Cellular and Molecular Biology Letters
|
1997
|
tom 02
|
nr 2
Incubation of soybean lipoxygenase isoenzymes (L-1, L-2, and L-3) with total resorcinolic lipids isolated from wheat bran or their purified homologs (5-n-pentadecylresorcinol and 5-n-tricosylresorcinol) led to apparent inhibition of all three isoenzyme activities. The IC50 values determined for studied compounds showed that the inhibitory activity was related to the length of the resorcinolic lipid aliphatic chain and was more effective for homolog with longer chain attached to 1,3-dihydroxybenzene ring in metha position. Similar dependence on the length of the alkylresorcinol side chain was observed also for Ki values. The 5-n-tricosylresorcinol (23:0 AR) was found to be the most efficient inhibitor of soybean lipoxygenases with IC50 values in the range of several µM regardless of the substrate used (linoleic acid or arachidonic acid). All alkylresorcinols studied caused increase of apparent KM values and decrease of VMAX values of the enzymes thus suggested the mixed type of lipoxygenase inhibition.
5

Interaction of alkylresorcinols with proteins

72%
Kozubek A.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 2
Alkylresorcinol homologs form stable monomolecular layers at air-water interface. Their interaction with proteins present in the subphase results in an increase of alkylresorcinol molecular packing in the extent dependent upon the protein studied. Strongest effects were observed for proteins with large hydrophobic regions, e.g. glycophorin or serum albumin. Interaction of proteins with alkylresorcinol monolayers is stronger than with phospholipids. A decrease and a shift of intrinsic protein fluorescence upon interaction with the compounds studied support their involvement in alteration of hydrophobic regions. For trypsin, 50% quenching was observed at the alkylresorcinol/trypsin ratio of 0.75. Concomitantly, an apparent inhibition of the enzymatic activity was noted. These results indicate that direct interaction of alkylresorcinols and modulation of enzymatic activities should be recognised as a significant part of the biological effect of these cereal bran components.
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