ascorbyl-monostearate and stearic-acid

ascorbyl-monostearate has been researched along with stearic-acid* in 1 studies

Other Studies

1 other study(ies) available for ascorbyl-monostearate and stearic-acid

Article	Year
Inhibition of human term placental and fetal liver glutathione-S-transferases by fatty acids and fatty acid esters. Toxicology letters, 1992, Volume: 60, Issue:3 Glutathione-S-transferase (GST) activity from human term placenta and human fetal liver towards 1-chloro-2,4-dinitrobenzene as the second substrate was significantly inhibited by the saturated fatty acids, stearic (SA) and palmitic (PA) acids and fatty acid esters, ascorbyl stearate (Asc-S) and ascorbyl palmitate (Asc-P). The nature of inhibition of human placental GST was competitive towards CDNB with Ki values of 3.1, 10.0, 13.5 and 18.5 microM for Asc-S, Asc-P, PA and SA, respectively. The inhibitory effect of Asc-S on human term placental GST was reversible. I50 values for Asc-S, Asc-P, SA and PA were 15, 45, 83 and 78 microM, respectively, for partially purified human fetal liver GSTs and 21, 6, 88 and 117 microM, respectively, for partially pure rat liver GSTs. The evidence suggests that Asc-S, Asc-P, SA and PA are potent inhibitors especially of the pi-class of GST. Topics: Animals; Ascorbic Acid; Female; Fetus; Glutathione Transferase; Humans; Isoenzymes; Kinetics; Labor, Obstetric; Liver; Palmitic Acid; Palmitic Acids; Placenta; Pregnancy; Rats; Stearic Acids	1992

Article

Year

Inhibition of human term placental and fetal liver glutathione-S-transferases by fatty acids and fatty acid esters.

Toxicology letters, 1992, Volume: 60, Issue:3

Glutathione-S-transferase (GST) activity from human term placenta and human fetal liver towards 1-chloro-2,4-dinitrobenzene as the second substrate was significantly inhibited by the saturated fatty acids, stearic (SA) and palmitic (PA) acids and fatty acid esters, ascorbyl stearate (Asc-S) and ascorbyl palmitate (Asc-P). The nature of inhibition of human placental GST was competitive towards CDNB with Ki values of 3.1, 10.0, 13.5 and 18.5 microM for Asc-S, Asc-P, PA and SA, respectively. The inhibitory effect of Asc-S on human term placental GST was reversible. I50 values for Asc-S, Asc-P, SA and PA were 15, 45, 83 and 78 microM, respectively, for partially purified human fetal liver GSTs and 21, 6, 88 and 117 microM, respectively, for partially pure rat liver GSTs. The evidence suggests that Asc-S, Asc-P, SA and PA are potent inhibitors especially of the pi-class of GST.

Topics: Animals; Ascorbic Acid; Female; Fetus; Glutathione Transferase; Humans; Isoenzymes; Kinetics; Labor, Obstetric; Liver; Palmitic Acid; Palmitic Acids; Placenta; Pregnancy; Rats; Stearic Acids

1992