Maggot kinase: A novel and cost-effective fibrinolytic enzyme from maggots.

Autor: Liu C; Key Laboratory for Northern Urban Agriculture of Ministry of Agriculture and Rural Affairs of China, Beijing University of Agriculture, Beijing 102206, PR China. Electronic address: liucan808@163.com., Sun H; Key Laboratory for Northern Urban Agriculture of Ministry of Agriculture and Rural Affairs of China, Beijing University of Agriculture, Beijing 102206, PR China., Zhang S; Key Laboratory for Northern Urban Agriculture of Ministry of Agriculture and Rural Affairs of China, Beijing University of Agriculture, Beijing 102206, PR China., Li X; Key Laboratory for Northern Urban Agriculture of Ministry of Agriculture and Rural Affairs of China, Beijing University of Agriculture, Beijing 102206, PR China., Ma L; Key Laboratory for Northern Urban Agriculture of Ministry of Agriculture and Rural Affairs of China, Beijing University of Agriculture, Beijing 102206, PR China; Beijing Advanced Innovation Center for Tree Breeding by Molecular Design, Beijing University of Agriculture, Beijing 102206, PR China. Electronic address: lqma@bua.edu.cn.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Dec; Vol. 282 (Pt 5), pp. 137350. Date of Electronic Publication: 2024 Nov 07.
DOI: 10.1016/j.ijbiomac.2024.137350
Abstrakt: Maggot kinase, a novel fibrinolytic enzyme source, has been isolated from fly maggots and comprehensively characterized. Using CM-52 ion exchange chromatography and affinity chromatography, we obtained a highly purified and active form of the enzyme. In particular, the fibrinolytic activity of maggot kinase, evaluated using the fibrin plate method, was found to be 8.98 ± 0.08 × 10 5  U/mg, demonstrating significant efficacy. Further structural analysis using mass spectrometry revealed that maggot kinase consists of a primary sequence of 226 amino acid residues with a molecular weight of 22.91 kDa. In vitro thrombolytic assays demonstrated the enzyme's remarkable ability to degrade the essential fibrinogen subunits (α, β, and γ), thereby facilitating clot lysis. Notably, our studies in a mouse model underscored the significant in vivo thrombolytic activity of maggot kinase, demonstrating its potential to inhibit thrombosis. The finding is particularly significant considering the widespread use of fly maggots in agriculture and animal husbandry due to their rapid growth cycle and minimal nutritional requirements. Our research highlights the untapped potential of fly maggots as a source for maggot kinase development for antithrombotic drug and functional food applications.
Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Can Liu, Lanqing Ma has patent licensed to Beijing University of Agriculture. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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