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通过使用三氟拉嗪作为去污剂从仙台病毒粒子中选择性提取血凝素和基质蛋白。

Selective extraction of haemagglutinin and matrix protein from Sendai virions by employing trifluoperazine as a detergent.

作者信息

Baiocchi M, Pescarmona M, Bruschi M L, Montecucco C, Squatriti T, Tomasi M

机构信息

Laboratorio di Biologia Cellulare, Istituto Superiore di Sanita, Roma, Italy.

出版信息

FEBS Lett. 1988 Sep 26;238(1):171-4. doi: 10.1016/0014-5793(88)80250-3.

Abstract

Incubation of trifluoperazine, a local anaesthetic, at concentrations higher than the cmc with Sendai virus particles produces the selective solubilization of the haemagglutinin neuraminidase (HN) and matrix (M) proteins. This phenomenon involves aggregation of the Sendai virions and therefore the separation of HN and M from the rest of the particle can be performed by bench centrifugation. The supernatant contains the HN and M proteins and HN, once inserted into liposomes, elicits its own biological activities. Therefore, the method seems suitable for purifying large amounts of HN.

摘要

将局部麻醉剂三氟拉嗪在高于临界胶束浓度(cmc)的浓度下与仙台病毒颗粒一起孵育,会导致血凝素神经氨酸酶(HN)和基质(M)蛋白的选择性溶解。这种现象涉及仙台病毒粒子的聚集,因此通过台式离心机即可将HN和M与颗粒的其他部分分离。上清液含有HN和M蛋白,并且HN一旦插入脂质体中,就会引发其自身的生物学活性。因此,该方法似乎适合大量纯化HN。

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