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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Si, Yue-Xiu Song, Jin-Jie Fang, Nai-Yun Wang, Wei Wang, Zhi-Jiang Yang, Jun-Mo Qian, Guo-Ying Yin, Shang-Jun Park, Yong-Doo |
| Description | Author Affiliation: Si YX ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.); Song JJ ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.); Fang NY ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.); Wang W ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.); Wang ZJ ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.); Yang JM ( Department of Dermatology, Sungkyunkwan University School of Medicine, Samsung Medical Center, Seoul 135-710, Republic of Korea.); Qian GY ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.); Yin SJ ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China. Electronic address: yinshangjun@163.com.); Park YD ( College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China) |
| Abstract | The regulation of enzymatic activity and unfolding studies of arginine kinase (AK) from various invertebrates have been the focus of investigation. To gain insight into the structural and folding mechanisms of AK from Euphausia superba (ESAK), we purified ESAK from muscle properly. The enzyme behaved as a monomeric protein with a molecular mass of about 40kDa and had pH and temperature optima of 8.0 and 30°C, respectively. The Km(Arg) and Km(ATP) for the synthesis of phosphoarginine were 0.30 and 0.47mM, respectively, and kcat/Km(Arg) was 282.7s(-1)/mM. A study of the inhibition kinetics of structural unfolding in the denaturant sodium dodecyl sulfate (SDS) was conducted. The results showed that ESAK was almost completely inactivated by 1.0mM SDS. The kinetics analyzed via time-interval measurements revealed that the inactivation was a first-order reaction, with the kinetic processes shifting from a monophase to biphase as SDS concentrations increased. Measurements of intrinsic and 1-anilinonaphthalene-8-sulfonate-binding fluorescence showed that SDS concentrations lower than 5mM did not induce conspicuous changes in tertiary structures, while higher concentrations of SDS exposed hydrophobic surfaces and induced conformational changes. These results confirmed that the active region of AK is more flexible than the overall enzyme molecule. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 67 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-06-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Arginine Kinase Chemistry Isolation & Purification Euphausiacea Enzymology Animals Metabolism Enzyme Stability Kinetics Protein Folding Temperature Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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