Feasibility of Sijunzi Tang (Chinese medicine) to enhance protein disulfide isomerase activities for reactivating malate dehydrogenase deactivated by polycyclic aromatic hydrocarbons
Autor: | Kwai Chung Cheung, Martin Tsz-Ki Tsui, Ken Kin Lam Yung, H. M. Leung, Wing Yin Mo, Yee Keung Wong, Yik Kit Yue, Chi Kin Au, Francis Siu Lai Kwok |
---|---|
Rok vydání: | 2018 |
Předmět: |
chemistry.chemical_classification
Molecular mass biology Chemistry Health Toxicology and Mutagenesis General Medicine 010501 environmental sciences 01 natural sciences Pollution Malate dehydrogenase Enzyme assay Ingredient chemistry.chemical_compound Enzyme Biochemistry biology.protein Environmental Chemistry Protein disulfide-isomerase Xenobiotic Carcinogen 0105 earth and related environmental sciences |
Zdroj: | Environmental Science and Pollution Research. 28:25116-25123 |
ISSN: | 1614-7499 0944-1344 |
Popis: | The objective of this research is to investigate the enzymatic activities between protein disulfide isomerase (PDI) found in animals and plants and the properties found in a commonly used Chinese medicine called Sijunzi Tang. During the investigation, PDI, which is a monomer with a molecular mass of 57.0 kDa, was used to reactivate malate dehydrogenase (MDH). However, with the interference of polycyclic aromatic hydrocarbons (PAHs), evidence indicates that such chemicals are carcinogenic, mutagenic, and toxic to humans. The enzymatic activity of PDI found in animal’s liver and plant was 1657 folds of purification; 0.284 unit/mg of enzyme activity, and 5694.4 folds of purification; 1.00 unit/mg of enzyme activity, respectively. PDI extracted in treated animal and plant tissue revealed 2.40% and 80.44% of regaining MDH enzymatic activity, respectively. Although in its initial phase of investigation, it is assumed that the properties found in Sijunzi Tang can help regain enzymatic activity in those affected by xenobiotic substances, thus, making it a potential ingredient in assisting with PDI functions. |
Databáze: | OpenAIRE |
Externí odkaz: |