Purification and proteomic analysis of potent fibrinolytic enzymes extracted from Lumbricus rubellus

Proteome Science

Research

Laurentia Stephani¹  Puji Rahayu¹  Raymond R. Tjandrawinata²  Maggy Thenawidjaja Suhartono³  Debbie Retnoningrum⁴  Heni Rachmawati⁴ 

[1] Biopharmaceutical Technology Division, Research Innovation and Invention, Dexa Laboratories of Biomolecular Sciences, PT Dexa Medica, Kawasan Industri Jababeka II, Industri Selatan V Block PP No. 7, 17550, Cikarang, Indonesia;Biopharmaceutical Technology Division, Research Innovation and Invention, Dexa Laboratories of Biomolecular Sciences, PT Dexa Medica, Kawasan Industri Jababeka II, Industri Selatan V Block PP No. 7, 17550, Cikarang, Indonesia;Faculty of Biotechnology, Atma Jaya Catholic University of Indonesia, Jalan Raya Cisauk-Lapan No. 10, 15345, Tangerang, Indonesia;Department of Food Science and Technology, Bogor Agricultural University, Fateta Building, Kampus IPB Darmaga, Bogor, Indonesia;Research Group of Pharmaceutics, School of Pharmacy, Bandung Institute of Technology, Bandung, Indonesia;

关键词: DLBS1033;    Earthworms fibrinolytic enzyme;    Lumbrokinase;    Lumbricus rubellus;    Protein purification;   

DOI  :  10.1186/s12953-023-00206-9

 received in 2022-11-08, accepted in 2023-04-16,  发布年份 2023

来源: Springer

【 摘 要 】

BackgroundLumbrokinase derived from earthworms, Lumbricus rubellus is known to have fibrinolytic enzymes that have potential as therapeutic drugs due to its ability to dissolve fibrin. The current study is aimed to purify the Lumbrokinase from L. rubellus and identify its protein component.MethodsWater extract of local earthworm Lumbricus rubellus revealed several proteins. Therefore, to identify its protein component, purification through HiPrep DEAE fast flow and proteomic analysis were conducted prior to identifications. A combination of two-dimension gel electrophoresis (2DE) and electrospray ionization mass spectrometry analysis was used to identify the purified fractions.ResultsThe purified fractions contain five protein bands, namely F25-1, F25-2, F85-1, F85-2, and F85-3, which displayed strong fibrinogenolytic activity. F25 fractions showed fibrinogenolytic activity of 974.85 U/mg, while F85 fractions showed higher activity of 1,484.11 U/mg. Fractions F85-1, F85-2, and F85-3 showed molecular weights of 42.6 kDa, 27.03 kDa, and 14 kDa, respectively and were identified as Lumbrokinase iso-enzymes.ConclusionThis preliminary study indicates that the F25 and F85 fractions are similar to published fibrinolytic protease-1 and lumbrokinase, respectively, in terms of their amino acid sequence.

【 授权许可】

CC BY   
© The Author(s) 2023

【 图 表 】

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