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A thermodynamic investigation on the binding of mercury ion with myelin basic protein at different temperatures

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Chinese Chemical Letters 2011年第5期22卷 623-625页

作者： G.Rezaei Behbehani L.Barzegar a.a.saboury S.Ghammami Chemistry Department Faculty of ScienceIslamic Azad UniversityTakestan BranchTakestanIran Institute of Biochemistry and Biophysics University of TehranTehranIran Department of Chemistry Imam Khomeini International UniversityQazvinIran

A thermodynamic study on the interaction of myelin basic protein with mercury ion was studied by using isothermal titration calonmetry,ITC,at 300.15,310.15 and 320.15 K in Tris buffer solution at pH *** enthalpies of MBP ＋ Hg^（2＋） interaction are reported and analysed in terms of the extended solvation *** was found that MBP has two identical and non-cooperative binding sites for Hg^（2＋） *** intrinsic dissociation equilibrium constants are 99.904,112.968 and 126.724μmol/L,and the molar enthalpy of binding are -11.634,-10.768 and -10.117kJ mol^（-1） at 300.15,310.15 and 320.15 K,respectively.

关键词： Myelin basic protein Mercury ion Isothermal titration calorimtry Binding parameters

Thermodynamic study of CN^- ion inhibition of Jack bean urease using the extended solvation theory

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Chinese Chemical Letters 2009年第11期20卷 1389-1392页

作者： G.Rezaei Behbehani a.a.saboury M.Mohebbian S.Tahmasbi Sarvestani M.Poorheravi Chemistry Department Imam Khomeini International UniversityQazvinIran Institute of Biochemistry and Biophysics University of TehranTehranIran Chemistry Department Payame Noor University(PNU)AbharIran

Cyanide ion was studied as an inhibitor of Jack bean urease at 300 K in 30 mmol/L tris buffer, pH 7. The inhibition was investigated by isothermal titration calorimetry （ITC）. The extended solvation model was used for CN^- ＋ JBU interaction over the whole range of CN^- concentrations. The binding parameters recovered from the solvation model were attributed to the cyanide ion interaction. It was found that cyanide ion acted as a non-cooperative inhibitor ofurease, and there is a set of 12 ± 0.12 identical and independent binding sites for CN- ions. The dissociation equilibrium constant is 749.99 umol/L. The molar enthalpy of binding is AH= -13.60 kJ mol^-1.

关键词： Jack bean urease Cyanide ion Isothermal titration calorimetry Binding parameters Inhibitor

Thermodynamic Studies on The Interaction of Nickel With Human Serum Albumin

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生物化学与生物物理进展 2003年第5期30卷 732-737页

作者： a.a.saboury F.HOSSEINI-KISHANI M.REZAEI-TAWIRANI B.RANJBAR Institute of Biochemistry and Biophysics University of ehranTehranIranInstitute of Biochemistry and BiophysicsUniversity of ehranTehranIranFaculty of MedicineMedical University of IlamIlamIranDepartment of BiologyUniversity of Tarbiat ModarresTehranIran

The interaction of human serum albumin with divalent nickel ion was studied by equilibrium dialysis, isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) and circular dichroism (CD) in 30 mmol/L Tris buffer , pH=7 0. There is a set of 8 identical binding sites for nickel binding on the protein at two temperatures of 300 K and 310 K. The cooperativity in the binding is observed at 310 K. The Hill coefficients at 300 K and 310 K are 0 97 and 1 25, respectively. The interaction between nickel ions and HSA is exothermic. A value of -36 5 kJ for enthalpy of interaction ( 1∶1 stoichiometry) was obtained. The secondary structure of HSA dose not show any change during the binding nickel ions process. However, the tertiary structure of the protein changes, which shows the existence of two natives like states.

关键词：热力学血清蛋白人类镍

氧化还原蛋白质在纳米簇功能膜修饰金电极上的直接电化学

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生物物理学报 2009年第S1期25卷 289-290页

作者：洪军 A.A.Mosavi-Movahedi H.Ghourchian a.a.saboury S.Rezaei-Zarchi 中国河南大学生命科学学院伊朗德黑兰大学生物化学与生物物理研究所

通过构建由 Nafion-核黄素组成的纳米簇功能膜,在此功能膜修饰的金电极上,实现了细胞色素 c、超氧歧化酶。

关键词：纳米簇功能膜修饰电极氧化还原蛋白质直接电化学

氧化还原蛋白质在纳米簇功能膜修饰金电极上的直接电化学

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氧化还原蛋白质在纳米簇功能膜修饰金电极上的直接电化学

Grassland Pasture Composition and Quality in the Communes of Ziguinchor and Kolda, Senegal

第十一次中国生物物理学术大会暨第九届全国会员代表大会

作者：洪军 A.A.Mosavi-Movahedi H.Ghourchian a.a.saboury S.Rezaei-Zarchi 中国河南大学生命科学学院伊朗德黑兰大学生物化学与生物物理研究所

＜正＞通过构建由Nafion-核黄素组成的纳米簇功能膜,在此功能膜修饰的金电极上,实现了细胞色素c、超氧歧化酶、辣根过氧化氢酶以及血红蛋白等氧化还原蛋白质的直接

关键词：纳米簇功能膜修饰电极氧化还原蛋白质直接电化学

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Open Journal of Ecology 2024年第9期14卷 683-705页

作者： Aly Diallo saboury Ndiaye Arfang Ousmane Kemo Goudiaby Yaya Diatta Mamadou Ndao Mamadou Diamanka Gnima Manga Department of Agroforestry Faculty of Science and Technology Assane Seck University of Ziguinchor Ziguinchor Senegal

In Senegal, natural pasture plays a major role in feeding livestock. During the rainy season, herbaceous plants account for a large proportion of the fodder consumed by ruminants. In Casamance, the composition and quality of these grasses are poorly known and underexploited. In this context, the study aimed to improve the knowledge and valorisation of the herbaceous fodder of the South. Individual interviews were conducted and a questionnaire was sent to farmers living in Ziguinchor and Kolda. A floristic inventory with a phytosociological approach was also carried out. The data collected were processed using Excel and Sphinx software in order to differentiate and classify the herbaceous species eaten by the tail. The majority of respondents were Fulani (55.30%). most of whom ranged in age from 30 to 60. Livestock rearing came second (38.3%) after agriculture (40%) among the principal activities of the people surveyed. The floristic inventory identified 95 species in 68 genera and 22 families. Species of low and medium pastoral value dominate the herbaceous layer. The global rangeland quality index was 48.16% and the brute pastoral value was 54.77%. Thirteen species contributed 54.86% of the pastoral value of the grassland. The floristic composition of community rangelands showed the presence of a varied herbaceous fodder range. The combination of which will help to develop a table of nutritional values for the formation of equilibrated feed rations for farmed livestock.

关键词： Fodder Herbaceous Pasture Nutritional Assessment Livestock

Covalent immobilization and characterization of Rhizopus oryzae lipase on core-shell cobalt ferrite nanoparticles for biodiesel production

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Chinese Journal of Chemical Engineering 2021年第9期34卷 128-136页

作者： Saboura Ashkevarian Jalil Badraghi Fatemeh Mamashli Behdad Delavari Ali Akbar saboury Research Institute of Applied Sciences ACECRShahid Beheshti UniversityTehranIran Institute of Biochemistry and Biophysics University of TehranTehranIran Center of Excellence in Biothermodynamics University of TehranTehranIran

Rhizopus oryzae lipase(ROL)was immobilized on the surface of silica coated amino modified CoFe_(2)O_4 nanoparticles and applied for biodiesel *** results indicated more affinity of the ROL toward its substrate upon immobilization,as revealed by a lower Km value for the immobilized ROL compared to its free *** fluorescence spectroscopy indicated a lower intensity for ROL immobilized on CoFe_(2)O_4 ***,immobilized ROL steady state anisotropy measurements presented lower values,which implied assembly of ROL molecules on magnetic nanoparticles upon immobilization as well as their restricted rotation upon covalent *** stability analysis revealed improved activity at higher temperatures for the immobilized enzyme compared to its free ***,Pace analysis to determine protein thermal stability revealed preservation of the protein conformation in the presence of increasing temperatures upon immobilization on ***,ROL immobilized on CoFe_(2)O_(4)nanoparticles exhibited improved efficiency of biodiesel production in agreement with thermal activity ***,the authors suggest application of the lipase molecules immobilized on CoFe_(2)O_(4)nanoparticles for more efficient biodiesel production.

关键词： Lipase immobilization CoFe_(2)O_(4)magnetic nanoparticles Steady state anisotropy Biodiesel Biocatalysis Protein stability

A Calorimetric Study on the Interaction of Zinc and Cadmium Ions with Jack Bean Urease

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Chinese Journal of Chemistry 2011年第3期29卷 446-450页

作者： Rezaei Behbehani, G. saboury, A. A. Sabbaghy, F. Chemistry Department Faculty of Science Islamic Azad University Takestan Branch Takestan Iran Institute of Biochemistry and Biophysics University ofTehran Tehran Iran Chemistry Department Payame Noor University (PNU) Abhar Iran

A thermodynamic study on the interaction of Jack bean urease, JBU, with Zn2＋ and Cd2＋ ions was studied by isothermal titration calorimetry （ITC） at 290, 300 and 310 K in 30 mmol/L Tris buffer solution, pH 7.0. The heats of JBU＋Zn2＋ and JBU＋Cd2＋ interactions are reported and analyzed in terms of the extended solvation theory. It was indicated that there is a set of 12 identical and non-interacting binding sites for Zn2＋ and Cd2＋ ions. The interactions of Zn2＋ and Cd2＋ ions with JBU are exothermic and both enthalpy and entropy driven. The association equilibrium constants for JBU＋Zn2＋ complexes are 4118.20, 3354.70 and 2790.62 Lomol 1 at 290, 300 and 310 K respectively. The association equilibrium constants for JBU＋Cd2＋ interactions are 2831.6 and 2386.28 Lomol 1 at 300 and 310 K, respectively.

关键词： jack bean urease isothermal titration calorimetry inhibitor zinc

A Microcalorimetry and Spectroscopy Study on the Interaction of BSA with 2,2′-Bipyridine Octylglycinato Palladium(II) Nitrate

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Acta Biochimica et Biophysica Sinica 2003年第10期35卷 886-890页

作者： MANSOORI-TORSHIZI Hassan,ISLAMI-MOGHADDAM Mahbobe,saboury Ali Akbar Institute of Biochemistry and Biophysics Department of Chemistry Institute of Biochemistry and Biophysics University of Tehran Tehran 14176-14411 Iran Department of Chemistry University of Sistan & Bluchestan Zahedan 98167-45345 Iran University of Sistan & Bluchestan Zahedan 98167-45345 Iran University of Tehran Tehran 14176-14411 Iran

The interaction of bovine serum albumin (BSA) with a new palladium(II) complex [Pd(bpy)(Oct-Gly)]NO 3 (bpy, 2,2′-bipyridine; Oct-Gly, octyl-glycine) was studied by isothermal titration UV-visible spectrophotometry and microcalorimetry in 30 mmol/L Tris buffer, pH 7.0. There is a set of 18 binding sites for this complex on BSA at 300 and 310 K with positive cooperativity in the binding process. The Hill coefficients at 300 and 310 K are 2.2 and 2.4, respectively. The binding of this palladium complex on BSA is endothermic with mean association binding constant of 21.0 and 16.4 (mmol/L) -1 at 300 and 310 K, respectively. The complex can denature the protein as surfactants. The stability of BSA in the interaction study with the complex is 84 and 58 kJ/mol at 300 and 310 K, respectively. Also, the enthalpy of BSA denaturation due to the interaction with the complex is 842 kJ/mol.

关键词： serum albumin palladium complex isothermal titration microcalorimetry spectrophotometry