http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Hamdi Riheb,Haik Yousef,Hayek Saleh S.,Samara Ayman,Mansour Said A. 한국물리학회 2021 Current Applied Physics Vol.28 No.-
Based on the evolution of the quantity of Sr in Pr0.63Dy0.37-xSrxMnO3 (x = 0.00 and x = 0.30) systems and the different heat treatments (500, 800 and 1300 ◦C), various physical changes are illustrated by these samples. Xray diffraction patterns were carried out revealing that the heat temperature can affect the structure of the systems. Zero-Field-Cooled and Field-Cooled magnetizations revealed the appearance of different magnetic transitions; from the paramagnetic state to the antiferromagnetic one. Once increasing the temperature of heat up to 1300 ◦C and for x = 0.30, the system presents a ferromagnetic order at Curie temperature that is around 200 K. Magnetic hysteresis loops confirm the transitions presented by the magnetic measurements. The heating temperature affected also the evolution of the magnetic entropy change. All samples show an important increase in the data values of the maximum of the magnetic entropy change while augmenting the applied magnetic field. We note an important result that is the refrigerant capacity of the x = 0.30 sample heated at 1300 ◦C is 725% compared to that at 500 ◦C.
Activity of Some Hepatic Enzymes in Schistosomiasis and Concomitant Alteration of Arylsulfatase B
( Mahmoud Balbaa ),( Mohamed El Kersh ),( Hamdy Mansour ),( Galila Yacout ),( Mohamed Ismail ),( Ahmed Malky ),( Khaled Bassiouny ),( Nihad Abdel Monem ),( Kamal Kandeel ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.2
The levels of arylsulfatases A and B, α-amylase, aspartate transcarbamylase, and γ-glutamyl transpeptidase were investigated during the infection of mice with schistosoma mansoni. This infection caused a significant (p<0.001) increase in the activity of hepatic arylsulfatases B (ASB), aspartate transcarbamylases and γ-glutamyl transpeptidase. A non-significant difference occurred for a-amylase (p<0.3) and arylsulfatases A(p>0.5) when compared to the control. The specific activity of hepatic ASB was progressively increased with the progression of the Schistosoma-infection. Moreover, the kinetic studies of hepatic ASB in Schistosoma-infection showed that a slight decrease in the value of K_(m) and about a 40% increase in V_(max) when compared to the control. In addition, the pH optimum of hepatic ASB was altered from 6 to 7 as a result of schistosomiasis. These observations suggest that there are schistosomiasis-associated changes of the catalytic and kinetic properties of hepatic ASB.
Activity of Some Hepatic Enzymes in Schistosomiasis and Concomitant Alteration of Arylsulfatase B
Balbaa, Mahmoud,El-Kersh, Mohamed,Mansour, Hamdy,Yacout, Galila,Ismail, Mohamed,Malky, Ahmed,Bassiouny, Khaled,Abdel-Monem, Nihad,Kandeel, Kamal Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.2
The levels of arylsulfatases A and B, $\alpha$-amylase, aspartate transcarbamylase, and $\gamma$-glutamyl transpeptidase were investigated during the infection of mice with schistosoma mansoni. This infection caused a significant (p<0.001) increase in the activity of hepatic arylsulfatase B (ASB), aspartate transcarbamylases and $\gamma$-glutamyl transpeptidase. A non-significant difference occurred for $\alpha$-amylase (p<0.3) and arylsulfatase A (p>0.5) when compared to the control. The specific activity of hepatic ASB was progressively increased with the progression of the Schistosoma-infection. Moreover, the kinetic studies of hepatic ASB in Schistosoma-infection showed that a slight decrease in the value of $K_m$ and about a 40% increase in $V_{max}$ when compared to the control. In addition, the pH optimum of hepatic ASB was altered from 6 to 7 as a result of schistosomiasis. These observations suggest that there are schistosomiasis-associated changes of the catalytic and kinetic properties of hepatic ASB.