Evidence map›Paper›PMID 30341759›Full record

ArticleEnvironmental science and pollution research international2021

Feasibility of Sijunzi Tang (Chinese medicine) to enhance protein disulfide isomerase activities for reactivating malate dehydrogenase deactivated by polycyclic aromatic hydrocarbons.

Ho Man Leung, Francis Siu Lai Kwok, Wing Yin Mo, Kwai Chung Cheung, Yik Kit Yue, Yee Keung Wong, Chi Kin Au, Martin Tsz Ki Tsui, Ken Kin Lam Yung

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Article in Environmental science and pollution research international, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

9 authors at 6 institutions in 3 countries.

Ho Man LeungDepartment of Biology, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China. hmhleung@hkbu.edu.hk.
Francis Siu Lai KwokDepartment of Applied Sciences, Institute of Vocational Education, Hong Kong, China.
Wing Yin MoDepartment of Science and Environmental Studies, The Hong Kong Education University, Tai Po, Hong Kong, China.
Kwai Chung CheungDepartment of Applied Sciences, Institute of Vocational Education, Hong Kong, China.
Yik Kit YueDepartment of Biology, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China.
Yee Keung WongSchool of Science and Technology, The Open University of Hong Kong, Ho Man Tin, Hong Kong.
Chi Kin AuDepartment of History, Hong Kong Shue Yan University, North Point, Hong Kong, China.
Martin Tsz Ki TsuiDepartment of Biology, University of North Carolina at Greensboro, Greensboro, NC, 27402, USA.
Ken Kin Lam YungDepartment of Biology, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China. kklyung@hkbu.edu.hk.
Hong Kong Baptist University · HKHong Kong Institute of Vocational Education · CNHong Kong Shue Yan University · CNEducation University of Hong Kong · HKHong Kong Metropolitan University · HKUniversity of North Carolina at Greensboro · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Polycyclic Aromatic HydrocarbonsProtein Disulfide-IsomerasesAnimalsFeasibility StudiesHumansMalate DehydrogenaseMedicine, Chinese TraditionalMalate DehydrogenasePolycyclic Aromatic HydrocarbonsProtein Disulfide-IsomerasesGlutathione reductase assayMalate dehydrogenase (MDH)Polycyclic aromatic hydrocarbons (PAHs)Protein disulfide isomerase (PDI)Sijunzi Tang

Identifiers

PMID30341759
OpenAlexW2896640421

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