A Protease from Moringa oleifera Lam. Exhibits In-vitro Blood Clot Solubilization and Fibrin Hydrolysis

IF 1.9 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

The Protein Journal Pub Date : 2024-07-28 DOI:10.1007/s10930-024-10222-z

Sawetaji, Kamal Krishan Aggarwal

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Abstract

Thrombosis is the formation of abnormal blood clots in the blood vessels that obstruct blood flow and lead to thrombosis. Current treatments for thrombosis are associated with serious side effects. Therefore there is a need for alternative natural therapy. A fibrinolytic protease was isolated from fresh leaves of Moringa oleifera Lam. and characterized for its potential to solubilize blood clots and hydrolyse fibrin under in-vitro conditions. The isolated protease showed a single protein band on native-PAGE. It showed optimum fibrinolytic activity at pH 8.0, 37 ^oC with 50 µg protein. The fibrinolytic activity of isolated protease was also confirmed by fibrin zymography. K_m and V_max of isolated protease were determined by the Lineweaver Burk plot. The isolated protease could solubilize 96.41% of blood clots by 96 h under in-vitro conditions. In-vitro fibrin hydrolysis and blood clot solubilization activities shown by an isolated protease from leaves of Moringa oleifera Lam. suggest its fibrinolytic potential to dissolve blood clots. Being a natural molecule and from a dietary plant it can be explored as an alternative natural therapy against thrombosis.

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从油辣木中提取的一种蛋白酶具有体外溶解血凝块和水解纤维蛋白的作用

血栓形成是指血管内形成异常血块，阻碍血液流动并导致血栓形成。目前治疗血栓的方法都有严重的副作用。因此，有必要寻找替代的自然疗法。从油辣木的新鲜叶子中分离出一种纤维蛋白溶解蛋白酶，并对其在体外条件下溶解血凝块和水解纤维蛋白的潜力进行了鉴定。分离出的蛋白酶在原生聚合酶链上显示出单一的蛋白质条带。它在 pH 值为 8.0、温度为 37 oC、蛋白质含量为 50 µg 时显示出最佳的纤维蛋白溶解活性。纤维蛋白酶谱也证实了分离蛋白酶的纤维蛋白溶解活性。分离蛋白酶的 Km 和 Vmax 是通过 Lineweaver Burk 图确定的。在体外条件下，分离蛋白酶可在 96 小时内溶解 96.41% 的血凝块。从油辣木叶片中分离出的蛋白酶所显示的体外纤维蛋白水解和血凝块溶解活性表明，它具有溶解血凝块的纤维蛋白溶解潜力。作为一种天然分子和食源性植物，它可以作为一种替代性自然疗法来治疗血栓形成。

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来源期刊

The Protein Journal 生物-生化与分子生物学

CiteScore

5.20

自引率

0.00%

发文量

审稿时长

12 months

期刊介绍： The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.