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novel fibrinolytic enzyme produced by bacillus sp. capable of dissolving the clots of pa6 fibrin

机译:芽孢杆菌产生的新型纤溶酶。能够溶解pa6纤维蛋白的凝块

摘要

the therapeutic approaches used today in response to vascular diseases include nonpharmacologic treatments (surgery, nutrition, pharmacology and therapeutics). these are essentially the antithrombotic agents and thrombolytic agents.the limitations of these traditional treatments have motivated the search for new drugs acting at different levels of the pathways of coagulation and fibrinolysis. new drugs of natural or synthetic origin have been developed in order to improve current treatments (choussat and montalescot, 1999).the present invention describes a novel fibrinolytic enzyme of pharmacological interest produced by the newly isolated strain of bacillus sp. 137 in the laboratory of enzyme engineering and microbiology (lgem), from the ground to a detergent plant.the enzyme of the invention has a main function to the destruction of fibrin clots under physiological conditions of ph, temperature and ion composition (ph 7.4; degree 2,68mm 136.9 mm nacl, kci, and 1.47 mm kh2po4, 8.1 mm na2hpo4). the enzyme of the invention is a serine protease with a molecular mass of 30 kda.the enzyme is active in a wide range of ph, with an optimum at ph 9.0 and recorded. the enzyme is active at temperatures ranging from 36 to 70 degrees c, with an optimum at only recorded after 10 min of incubation. however, the enzyme is very unstable at high temperature. the time of 1 / 2 to 60 degrees c is only 3 minutes, so that no loss of activity was observed after 1h incubation at 37oc.the study of the stability of the enzyme of the invention under physiological conditions of ph, temperature and ionic composition shows that it is very stable. the enzyme is more than 95% of its activity after 5 hours of incubation at 37oc.
机译:当今用于应对血管疾病的治疗方法包括非药物治疗(手术,营养,药理学和治疗学)。这些传统疗法的局限性促使人们寻求在不同水平的凝血和纤溶途径中起作用的新药。为了改善当前的治疗,已经开发了天然或合成来源的新药物(choussat和montalescot,1999)。本发明描述了由新分离的芽孢杆菌属菌株产生的具有药理学意义的新型纤溶酶。 137在酶工程和微生物学实验室(lgem)中,从地面到去污植物。本发明的酶具有在pH,温度和离子组成的生理条件下破坏血纤蛋白凝块的主要功能(pH 7.4;度为2,68毫米,136.9毫米Nacl,kci和1.47毫米kh2po4、8.1毫米na2hpo4。本发明的酶是分子量为30kda的丝氨酸蛋白酶。该酶在广泛的ph范围内具有活性,最适pH为9.0,并被记录。该酶在36至70摄氏度的温度范围内具有活性,只有在孵育10分钟后才能记录到最佳温度。然而,该酶在高温下非常不稳定。 1/2至60摄氏度的时间仅为3分钟,因此在37℃孵育1小时后未观察到活性损失。研究在pH,温度和离子生理条件下本发明酶的稳定性组成表明它非常稳定。在37oC下孵育5小时后,该酶的活性超过其活性的95%。

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