Madhu, C. S. and Srinivas, Balaji K. and Jayarama, S. (2017) Haemostatic property of new Cystein protease(s) from Sesbania grandiflora: It's action on fibrinogens. Biocatalysis and Agricultural Biotechnology, 12. 10 - 14. ISSN 1878-8181
Full text not available from this repository. (Request a copy)Abstract
This study aims to explore possible involvement of Sesbania grandiflora leaves extract on haemostatic pathway. The crude dialyzed fraction (SgCDF) hydrolyses casein and exhibiting a protease activity (19.7 ± 1.5U/Hr) at 100μg/ml. Zymography (casein) studies further reveal the presence of two high molecular weight protease(s). Presence of possible protease(s) was confirmed by inhibition of Proteolytic activity by mercury chloride (HgCl2) suggesting the presence of Cysteine protease. The stability of protease activity against various parameters viz., temperature, pH, salt (NaCl) has been evaluated. These protease(s) exhibiting a promising Fibrinogenolytic activity by hydrolyzing Aα and Bβ subunit of fibrinogen at 25μg and 50μg concentration, whereas SgCDF fails to degrade the γ-subunit at the same concentration. The protease shows a promising recalcification time up to 80 ± 2 against Trypsin. These findings suggest the possible role of proteolytic fraction of Sesbania grandiflora in haemostatic and wound healing process.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Hemostasis, Procoagulant, Cystein protease, Fibrinogen |
| Subjects: | C Chemical Science > Biochemistry |
| Divisions: | Yuvaraj college > Bio-Chemistry |
| Depositing User: | C Swapna Library Assistant |
| Date Deposited: | 03 Jul 2019 06:32 |
| Last Modified: | 03 Jul 2019 06:32 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/4563 |
Actions (login required)
 |
View Item |
