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

Authors :
Laurentia Stephani
Puji Rahayu
Debbie Retnoningrum
Maggy Thenawidjaja Suhartono
Heni Rachmawati
Raymond R. Tjandrawinata
Source :
Proteome Science, Vol 21, Iss 1, Pp 1-10 (2023)
Publication Year :
2023
Publisher :
BMC, 2023.

Abstract

Abstract Background Lumbrokinase 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. Methods Water 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. Results The 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. Conclusion This 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.

Details

Language :
English
ISSN :
14775956
Volume :
21
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Proteome Science
Publication Type :
Academic Journal
Accession number :
edsdoj.f004493db4834b05b4b2ed087a27d2e8
Document Type :
article
Full Text :
https://doi.org/10.1186/s12953-023-00206-9