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目的:从螺旋藻发酵物中纯化出螺旋藻激酶,并通过质谱分析其蛋白相关信息,为研究其结构和功能提供理论依据。方法:通过切向超滤法、Sephadex G-75凝胶色谱层析、超滤离心管离心法、SDS-PAGE电泳法从螺旋藻发酵物中纯化出螺旋藻激酶,通过基质辅助激光解析电离飞行时间质谱技术分析其蛋白相关信息。结果:获得纯化的单一螺旋藻激酶,其相对分子质量约为45 000,能直接溶解纤维蛋白。基质辅助激光解析电离飞行时间质谱分析表明螺旋藻激酶的氨基酸序列与极大节螺旋藻犬尿氨酸甲酰胺酶有较高相似度,蛋白覆盖率为35%。结论:从螺旋藻发酵物中成功纯化出螺旋藻激酶,并通过质谱获得其蛋白相关信息。
Objective: To purify Spirulina platensis from spirulina fermentation material and analyze its protein-related information by mass spectrometry to provide a theoretical basis for studying its structure and function. METHODS: Spirulina platensis was purified from spirulina fermentations by tangential ultrafiltration, Sephadex G-75 gel chromatography, ultrafiltration centrifugation, and SDS-PAGE electrophoresis. Matrix-assisted laser desorption/ionization flight was performed. Time-mass spectrometry analyzes its protein-related information. Results: A purified single spirulina kinase with a relative molecular weight of approximately 45,000 was obtained, which directly dissolved fibrin. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis showed that the amino acid sequence of Spirulina platensis had a high degree of similarity with the maximal K. pulcherrima ureaminolformamidase with a protein coverage of 35%. CONCLUSION: Spirulina platensis was successfully purified from the spirulina fermentation product and its protein-related information was obtained by mass spectrometry.