Mimusops elengi (Bakula) Gelatinolytic Protease and its Plasmin-like Action on the Blood Clot.

Autor:	Gowda NGS; Division of Biochemistry, School of Life Sciences, JSS Academy of Higher Education & Research, Mysuru-570 015, Karnataka, India.; Department of Biochemistry, Center of Excellence in Molecular Biology & Regenerative Medicine, JSS Medical College, JSS Academy of Higher Education and Research, Mysuru-570 015, India., Raju NR; Division of Biochemistry, School of Life Sciences, JSS Academy of Higher Education & Research, Mysuru-570 015, Karnataka, India., Silina E; Department of Human Pathology, Institute of Biodesign and Modeling of Complex Systems, I.M. Sechenov First Moscow State Medical University (Sechenov University), Trubetskaya St., 8, Moscow, 119991, Russia., Stupin V; Department of Hospital Surgery, N.I. Pirogov Russian National Research Medical University (RNRMU), Ostrovityanova St. 1, Moscow, 119991, Russia., Achar RR; Division of Biochemistry, School of Life Sciences, JSS Academy of Higher Education & Research, Mysuru-570 015, Karnataka, India.
Jazyk:	angličtina
Zdroj:	Current protein & peptide science [Curr Protein Pept Sci] 2022; Vol. 23 (10), pp. 706-712.
DOI:	10.2174/1389203723666220829114301
Abstrakt:	Background: Mimusops elengi, popularly known as Bakula in Ayurvedic Medicine, is a member of the Sapotaceae family. Concerning the traditional and Ayurvedic medicinal use of Mimusops elengi leaves, especially in wound healing and oral care, the plausible presence of proteolytic activity in an aqueous Mimusops elengi leaf extract was investigated in our study. Methods: Mimusops elengi Gelatinolytic Protease was named after fractioning the extract. The Zymogram assay validated the gelatin specificity. The effect of MEGP on the wound healing process was investigated using a different assay. Results: The presence of protease with gelatinolytic & caseinolytic activity at 62.53±1.43 U/h and 15.31±0.64 U/h, respectively. The aqueous enzyme fraction was named Mimusops elengi Gelatinolytic Protease (MEGP). The specificity of gelatin was confirmed by zymogram. Gelatinolytic activity of MEGP was also higher than that of trypsin at 27.96±0.38 U/h. MEGP was 49.14±1.61 % inhibited by PMSF, indicating the predominant presence of serine proteases. The optimal pH and temperature for MEGP were found to be 8 and 37°C, implying that it is an alkaline protease. MEGP dissolved the blood clot at a rate of 8.41±1.04 U/h, which is higher than the trypsin clot-dissolving rate of 1.027±0.04 U/h. The plasma clot hydrolytic capacity is confirmed when MEGP hydrolyzes alpha-polymer subunits in a dose-dependent manner. Conclusion: This investigation shows that MEGP has a plasmin-like activity that possesses a significant role in clot disintegration and other wound ailments, warranting its use in traditional Indian medicine. (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.)
Databáze:	MEDLINE
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