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首页> 外文期刊>Protein Expression and Purification >Heterologous expression of Mytilus californianus foot protein three (Mcfp-3) in Kluyveromyces lactis
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Heterologous expression of Mytilus californianus foot protein three (Mcfp-3) in Kluyveromyces lactis

机译：乳酸克鲁维酵母中Mytilus californianus足蛋白3（Mcfp-3）的异源表达

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摘要

Mytilus califorianus foot protein three (Mcfp-3) was successfully expressed in the yeast, Kluyveromyces lactis. The first nine amino acids (YPYDVPDYA) from the hunian-influenza-virus hemagglutinin (HA) protein were fused to the amino terminus of Mcfp-3 (HA-Mcfp-3) to facilitate identification and purification. HA-Mcfp-3 was purified to a concentration of 1 mg/L using HA affinity chromatography. The recovered polypeptide was resolved by SDS-PAGE and migrated primarily at 36 kDa, an increase of approximately 29 kDa over the calculated molecular weight of a HA-Mcfp-3 monomer. Significantly, release of Mcfp-3 by enterokinase treatment coincided with the formation of high molecular weight complexes. It is noteworthy that the complexes mimicked the previously reported insolubility of Mcfps found in vivo to denaturing and reducing conditions. These data demonstrate the successful expression of Mcfp-3 in K lactis and show an intrinsic ability of Mcfp-3 to self-assemble into stable, higher molecular weight forms. (c) 2007 Elsevier Inc. All rights reserved.
机译：在酵母乳酸克鲁维酵母中成功表达了Mytilus califorianus足蛋白3（Mcfp-3）。来自禽流感病毒血凝素（HA）蛋白的前九个氨基酸（YPYDVPDYA）与Mcfp-3（HA-Mcfp-3）的氨基末端融合，以方便鉴定和纯化。使用HA亲和色谱将HA-Mcfp-3纯化至1 mg / L的浓度。回收的多肽通过SDS-PAGE解析，并主要以36 kDa迁移，与HA-Mcfp-3单体的计算分子量相比增加了约29 kDa。值得注意的是，通过肠激酶处理释放的Mcfp-3与高分子量复合物的形成相吻合。值得注意的是，该复合物模仿了先前报道的体内发现的Mcfps不变性和还原条件的不溶性。这些数据证明了Mcfp-3在乳酸乳球菌中的成功表达，并显示了Mcfp-3自组装成稳定的更高分子量形式的内在能力。 （c）2007 Elsevier Inc.保留所有权利。

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