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Partial Characterization of Protein Extracted from Terminalia catappa Seed Behaving as Lectin that is Capable of Mouse Sperm Agglutination

机译:从末端血管素Catappa种子中提取的蛋白质的部分表征表现为能够凝集凝集素的凝集素

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The objective of this research is to partially characterize proteins extracted from Terminalia catappa seeds that behave like lectin, being capable of mouse sperm agglutination. Cotyledons of the seed were extracted in homogenizing PBS buffer. The supernatant was precipitated with ammonium sulfate to a final concentration of 50% (w/v), then dialyzed with 2 kinds of dialysis tubes, i.e. 6000 and 12000 MWCO. The precipitated proteins were then diluted in 0.9% (w/v) NaCl. Next, dialysis fractions of the precipitated protein were used for the mouse sperm agglutination test. Protein from the dialysis fraction of 6000 MWCO tube could agglutinate mouse sperm. The quantitation of protein was carried out by using the Bradford Coomassie kit from crude extract to dialyzed fractions. Both dialyzed fractions were also run on SDS-PAGE to see the protein profiles.
机译:该研究的目的是部分地表征从终端炎Catappa种子中提取的蛋白质表征,该蛋白质表现出凝集素,能够进行小鼠精子凝集。在均质化PBS缓冲液中提取种子的子叶。将上清液用硫酸铵沉淀至终浓度为50%(w / v),然后用2种透析管透析,即6000和12000 mwco。然后将沉淀的蛋白质以0.9%(w / v)NaCl稀释。接下来,使用沉淀蛋白的透析级分用于小鼠精子凝集试验。来自6000 MWCO管的透析级分的蛋白质可以凝集小鼠精子。通过使用来自粗提物的Bradford Coomassie套件对透析级分来进行蛋白质的定量。在SDS-PAGE上也会在SDS-PAGE上进行透析级分,看看蛋白质谱。

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