检索结果-南通市图书馆

Unfolding and Inactivation of Green Crab (Scylla Serrata) Alkaline Phosphatase during thermal denaturation

Tsinghua Science and Technology 1998年第3期3卷 9-12页

作者：陈清西赵红张伟杨黄浩张彤周海梦 Department of Biology Xiamen University Xiamen 361005 Department of Biological Science and Biotechnology Tsinghua University Beijing 100084

Enzyme activity is strongly dependent on its conformational integrity. The present paper compares the inactivation and unfolding of green crab (Scylla serrata) alkaline phosphate during thermal denaturation. The results show that inactivation takes place before noticeable conformational changes. This is in general accord with the suggestion previously made by Tsou, indicating that the active site of multi metal enzymes is situated in a region more flexible than the molecules as a whole. 

关键词： alkaline phosphatase green crab thermal denaturation inactivation unfolding

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

Different Thermostability of Skeletal Muscle Glyceraldehyde-3-phosphate Dehydrogenase from Hibernating and Euthermic Jerboa (Jaculus orientalis)

引用

Acta Biochimica et Biophysica Sinica 2003年第10期35卷 891-896页

作者： IDDAR Abdelghani,CAMPOS Luis A.,SANCHO Javier,SERRANO Aurelio,SOUKRI Abdelaziz Laboratoire de Biochimie Departamento de Bioquímica y Biología Molecular y Celular Departamento de Bioquímica y Biología Molecular y Celular Instituto de Bioquímica Vegetal y Fotosíntesis Laboratoire de Biochimie Unitè de Gènie Enzymatique et Biologie Molèculaire Facultè des Sciences-Ain Chock Casablanca Morocco Universidad de Zaragoza Zaragoza Spain Universidad de Zaragoza Zaragoza Spain CSIC-Universidad de Sevilla Sevilla Spain Unitè de Gènie Enzymatique et Biologie Molèculaire Facultè des Sciences-Ain Chock Casablanca Morocco

In previous study, we demonstrated that the specific activity of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.***.1.12) in skeletal muscle of induced hibernating jerboa (hibernating GAPDH) was 3-4 folds lower than that of the one in the skeletal muscle of the euthermic jerboa (euthermic GAPDH). A significant decrease in both GAPDH protein and GapC mRNA levels occurs when hibernating, but the purified hibernating GAPDH is less active than the euthermic GAPDH. To investigate the physico-chemical basis of this lower activity, the behaviour during thermal inactivation of skeletal muscle GAPDH from hibernating and euthermic tissues was examined by a variety of spectroscopic techniques, including fluorescence emission, circular dichroism and ultraviolet absorption. A clear resistance to thermal denaturation was observed in the hibernating GAPDH compared with the euthermic GAPDH. The different temperature of denaturation found in these proteins by both fluorimetry and circular dichroism indicates that there might exist conformational changes of GAPDH upon hibernation that could affect the stability of this enzyme.

关键词： glyceraldehyde-3-phosphate dehydrogenase hibernation thermal denaturation circular dichroism spectroscopy protein stability

来源：

同方期刊数据库评论

在线全文

同方期刊数据库

学校读者我要写书评

暂无评论

Analysis of Lattice Size, Energy Density and denaturation for a One-Dimensional DNA Model

引用

World Journal of Mechanics 2012年第2期2卷 84-89页

作者： Gabriel Gouvea Slade Natalia Favaro Ribeiro Elso Drigo Filho Jose Roberto Ruggiero Department of Physics Sao Paulo State UniversitySao Josédo Rio PretoBrazil

There are several mechanical models to describe the DNA phenomenology. In this work the DNA denaturation is studied under thermodynamical and dynamical point of view using the well known Peyrard-Bishop model. The thermodynamics analysis using the transfer integral operator method is briefly reviewed. In particular, the lattice size is discussed and a conjecture about the minimum energy to denaturation is proposed. In terms of the dynamical aspects of the model, the equations of motion for the system are integrated and the results determine the energy density where the denatura- tion occurs. The behavior of the lattice near the phase transition is analyzed. The relation between the thermodynamical and dynamical results is discussed.

关键词： DNA Mechanical Model Peyrard-Bishop Model Lattice Size thermal denaturation

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

Two Ways of denaturation Leading to Different Transition States of Fibrinogen

引用

Tsinghua Science and Technology 1997年第1期2卷 69-73页

作者：赵南明公衍道李菲张秀芳 Department of Biological Science and Biotechnology State Key Laboratory of Biomembrane and Membrane Biotechnology Tsinghua University Beijing 100084

HFG (human fibrinogen) desorbed from a PTFE (polytetrafluoroethylene) surface and thermally denatured HFG were conformationally studied by using FTIR (Fourier transform infrared) spectroscopy. It is shown that some irreversible conformational changes of HFG, including a decrease in the α helix content and an increase in the β structure content, were induced by the PTFE surface adsorption/*** suggests that some α helix structures should transform into β *** HFG was thermally denatured as well as the native HFG under a thermal incubation of 30 min at 73 ℃ .After the same thermal treatment, the α helix content in the thermally denatured desorbed HFG was obviously less than that in the former native HFG.

关键词： human fibrinogen (HFG) polytetrafluoroethylene (PTFE) thermal denaturation adsorption/desorption

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

thermal Unfolding of Escherichia oli Trigger Factor Studied by Ultra-Sensitive Differential Scanning Calorimetry

Thermal Unfolding of Escherichia oli Trigger Factor Studied ...

引用

第九届全国酶学学术讨论会暨邹承鲁诞辰85周年纪念会

作者： Dong-Jie Fan Yan-Wei Ding Xian-Ming Pan Jun-Mei Zhou National Laboratory of Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences,15 Datun Road,Beijing 100101,China.Hefei National Laboratory for Physical Science at Microscale,University of Science and Technology of China,Hefei,230026.Graduate School of the Chinese Academy of Sciences,19 Yuquan Road,Shijinshan District,Beijing 100039,China

Escherichia coli trigger factor (TF) is an important molecular chaperone in nascent peptide *** binds at the ribosome exit tunnel through the interaction of the highly flexible loop in its N-terminal domain with the L... 详细信息

关键词： cross-linking DSC intermediate folding thermal denaturation trigger factor

来源： cnki会议评论

在线全文

cnki会议

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：