The photon-induced processes at the LHC provide clean experimental conditions due to absence of theproton remnants,which might produce complementary and interesting results for tests of the standard model and forsearc...The photon-induced processes at the LHC provide clean experimental conditions due to absence of theproton remnants,which might produce complementary and interesting results for tests of the standard model and forsearching of new physics.In the context of the littlest Higgs model with T-parity,we consider the photon-inducedproduction of the mirror quarks at the LHC.The cross sections for various production channels are calculated and asimply phenomenological analysis is performed by assuming leptonic decays.展开更多
Spermidine or spermine but not putrescine inhibited progesterone induced Bufo bufo gargarizans oocyte maturation.The ID50 for spermine inhibition via intra -oocyte microinjection on maturation induced by progesterone ...Spermidine or spermine but not putrescine inhibited progesterone induced Bufo bufo gargarizans oocyte maturation.The ID50 for spermine inhibition via intra -oocyte microinjection on maturation induced by progesterone was 6.8mM(100nl).Spermine could inhibit MPF induced toad oocyte maturation with a much higher ID50.A 55 kD protein was dephosphorylated during the process of progesterone induced oocyte maturation .Spermine selectively promoted the level of phosphorylation of this protein in both progesterone-stimulated and hormone-untreated oocytes.The extent of its dephosphorylation was fairly Correlated with the percentage of GVBD in the hormone stimulated oocytes.The level of endogenous spermine was reduced by 28% between the perod of 0.40 GVBD50 and 0.60 GVBD50,at which 55 kD protein was dephosphorylated.Spermine inhibited progesterone-stimulated protein synthesis in almost the same dose dependent manner as its inhititory effect on the hormone-induced maturation,The endogenous spermine regulated 55 kD protein dephosphorylation which may trigger the increase of protein dephosphorylation which may trigger the increase of protein synthesis and in turn promote the activation of MPF,It is possible that 55 kD protein may be one of the components of messenger ribonucleoprotein(mRNP) particles.展开更多
基金Supported in part by the National Natural Science Foundation of China under Grant No.10675057the Natural Science Foundation of the Liaoning Scientific Committee under Grant No.20082148Foundation of Liaoning Educational Committee under Grant No.2007T086
文摘The photon-induced processes at the LHC provide clean experimental conditions due to absence of theproton remnants,which might produce complementary and interesting results for tests of the standard model and forsearching of new physics.In the context of the littlest Higgs model with T-parity,we consider the photon-inducedproduction of the mirror quarks at the LHC.The cross sections for various production channels are calculated and asimply phenomenological analysis is performed by assuming leptonic decays.
文摘Spermidine or spermine but not putrescine inhibited progesterone induced Bufo bufo gargarizans oocyte maturation.The ID50 for spermine inhibition via intra -oocyte microinjection on maturation induced by progesterone was 6.8mM(100nl).Spermine could inhibit MPF induced toad oocyte maturation with a much higher ID50.A 55 kD protein was dephosphorylated during the process of progesterone induced oocyte maturation .Spermine selectively promoted the level of phosphorylation of this protein in both progesterone-stimulated and hormone-untreated oocytes.The extent of its dephosphorylation was fairly Correlated with the percentage of GVBD in the hormone stimulated oocytes.The level of endogenous spermine was reduced by 28% between the perod of 0.40 GVBD50 and 0.60 GVBD50,at which 55 kD protein was dephosphorylated.Spermine inhibited progesterone-stimulated protein synthesis in almost the same dose dependent manner as its inhititory effect on the hormone-induced maturation,The endogenous spermine regulated 55 kD protein dephosphorylation which may trigger the increase of protein dephosphorylation which may trigger the increase of protein synthesis and in turn promote the activation of MPF,It is possible that 55 kD protein may be one of the components of messenger ribonucleoprotein(mRNP) particles.
