Publication: A protein from aloe vera that inhibits the cleavage of human fibrin(ogen) by plasmin
Issued Date
2013-08-01
Resource Type
ISSN
15590291
02732289
02732289
Other identifier(s)
2-s2.0-84881314617
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Mahidol University
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SCOPUS
Bibliographic Citation
Applied Biochemistry and Biotechnology. Vol.170, No.8 (2013), 2034-2045
Suggested Citation
Jaruwan Siritapetawee, Punchapat Sojikul, Siriwat Soontaranon, Wanwisa Limphirat, Sompong Thammasirirak A protein from aloe vera that inhibits the cleavage of human fibrin(ogen) by plasmin. Applied Biochemistry and Biotechnology. Vol.170, No.8 (2013), 2034-2045. doi:10.1007/s12010-013-0356-2 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/31269
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Title
A protein from aloe vera that inhibits the cleavage of human fibrin(ogen) by plasmin
Abstract
A protease inhibitor protein with the molecular mass of 11,804.931 Da (analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry) was isolated from Aloe vera leaf gel and designated as AVPI-12. The isoelectric point of the protein is about 7.43. The first ten amino acid sequence from the N-terminal was found to be R-D-W-A-E-P-N-D-G-Y, which did not match other protease inhibitors in database searches and other publications, indicating AVPI-12 is a novel protease inhibitor. The band protein of AVPI-12 migrated further on nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) than reducing SDS-PAGE. This result indicated that the molecule of AVPI-12 did not contain interchain disulfide bonds, but appeared to have intrachain disulfide bonds instead. AVPI-12 strongly resisted digestion by the serine proteases human plasmin and bovine trypsin. The protein could protect the γ-subunit of human fibrinogen from plasmin and trypsin digestion, similar to the natural plasma serine protease inhibitor α2-macroglobulin. The protein also could protect the γ-subunit of fibrinogen from the cysteine protease papain. AVPI-12 also exhibited dose-dependent inhibition of the fibrinogenolytic activity of plasmin, similar to α2-macroglobulin. The fibrinolytic inhibitory activity of AVPI-12 and the small-angle X-ray scattering showed that the protein could protect human fibrin clot from complete degradation by plasmin. The inhibition of the fibrinogenolytic and fibrinolytic activities of plasmin by AVPI-12 suggests that the inhibitor has potential for use in antifibrinolytic treatment. © 2013 Springer Science+Business Media New York.