Derivative spectrophotometry of dimer and monomer of enolase期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Derivative spectrophotometry of dimer and monomer of enolase

Affiliation:	1. Medical Bionanotechnology, Faculty of Allied Health Sciences, Chettinad Hospital and Research Institute, Chettinad Academy of Research and Education, Chettinad Health City, Rajiv Gandhi Salai, Kelambakkam, Tamilnadu 603103, India;2. Department of Anesthesiology, Rutgers University, Newark, New Jersey 07103, United States of America;1. Virginia Tech Carilion Research Institute and School of Medicine, Roanoke, VA, USA;2. Graduate Program in Translational Biology, Medicine, and Health, Virginia Tech, Blacksburg, VA, USA;3. Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA;4. Center for Heart and Regenerative Medicine, Virginia Tech Carilion Research Institute, Roanoke, VA, USA

Abstract:	1.1. SDS causes significant polar exposure of aromatic amino acids of enolase. The α-helix content remains unchanged. The enzyme lost all its activity. 2.2. The presence of 1 M KBr in enzyme solution results in a smaller increase of polarity of aromatic amino acids residues environment. The amount of α-helix does not decrease in comparison to native enzyme. Enzyme lost nearly 80% of its initial activity. 3.3. The extreme pH values and the presence of 6 M Gnd.HCl influence the whole structure of enolase. It is accompanied by a large polar shift of aromatic amino acids and significant decrease of α-helix content of the protein.

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