In this work the hydrolysis rate constants(k) of a series of Aliphatic esters in different concent of ethanol solution were studied by conductometry,and some correlative analysis were done about the relation among the...In this work the hydrolysis rate constants(k) of a series of Aliphatic esters in different concent of ethanol solution were studied by conductometry,and some correlative analysis were done about the relation among the molecular structure of a series of Aliphatic esters,thecondition of hydrolysis and hydrolysis rate constants(k).The quantificational mathematic equation:lgk=a+blg PEI(R)+clgε,among hydrolysis rate constants(k),the polarizability effect index(PEI) of alkyl group(R)and dielectric constant(ε) and this behavior was deduced.Simultaneously,the effect of FOS on hydrolysis rate constants(k) of Aliphatic esters in 39.9%(v/v) ethanol solution were measured in above meaning.The quantificational mathematic expression between hydrolysis rate constants(k) of ester and the concentration of FOS(M):k=k′/(1+AM),was deduced and validated.The result showed that FOS inhibited the hydrolysis reaction of Aliphatic esters.展开更多
A study is made on the previously ignored problem of the dependence of a static fluorescence quenching Stern-Volmer constant?Ksv on the initial concentration of [F]0 fluorophore F. This correlation is shown to exist. ...A study is made on the previously ignored problem of the dependence of a static fluorescence quenching Stern-Volmer constant?Ksv on the initial concentration of [F]0 fluorophore F. This correlation is shown to exist. It is concluded that the Stern-Volmer quenching constant may be used as association constant K only with .展开更多
Bioassay based on the luminescent bacteria was used as a new method for the determination of the kinetic constants of ligand binding to the complexion agent. Miramistin as the cationic surface-active antiseptic and se...Bioassay based on the luminescent bacteria was used as a new method for the determination of the kinetic constants of ligand binding to the complexion agent. Miramistin as the cationic surface-active antiseptic and serum blood albumin was taken as a model of interacting agent’s. It was concluded that this approach might have a wide range for applications, namely, in all cases where the ligand is an inhibitor of bacterial luminescence and its complex dose not effect the intensity of this process.展开更多
文摘In this work the hydrolysis rate constants(k) of a series of Aliphatic esters in different concent of ethanol solution were studied by conductometry,and some correlative analysis were done about the relation among the molecular structure of a series of Aliphatic esters,thecondition of hydrolysis and hydrolysis rate constants(k).The quantificational mathematic equation:lgk=a+blg PEI(R)+clgε,among hydrolysis rate constants(k),the polarizability effect index(PEI) of alkyl group(R)and dielectric constant(ε) and this behavior was deduced.Simultaneously,the effect of FOS on hydrolysis rate constants(k) of Aliphatic esters in 39.9%(v/v) ethanol solution were measured in above meaning.The quantificational mathematic expression between hydrolysis rate constants(k) of ester and the concentration of FOS(M):k=k′/(1+AM),was deduced and validated.The result showed that FOS inhibited the hydrolysis reaction of Aliphatic esters.
文摘A study is made on the previously ignored problem of the dependence of a static fluorescence quenching Stern-Volmer constant?Ksv on the initial concentration of [F]0 fluorophore F. This correlation is shown to exist. It is concluded that the Stern-Volmer quenching constant may be used as association constant K only with .
文摘Bioassay based on the luminescent bacteria was used as a new method for the determination of the kinetic constants of ligand binding to the complexion agent. Miramistin as the cationic surface-active antiseptic and serum blood albumin was taken as a model of interacting agent’s. It was concluded that this approach might have a wide range for applications, namely, in all cases where the ligand is an inhibitor of bacterial luminescence and its complex dose not effect the intensity of this process.
