瓶鼻海豚（Tursiops truncatus）重组表面活性蛋白 D 的表达和基本生化特征。

IF 1.4 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Protein expression and purification Pub Date : 2024-06-15 DOI:10.1016/j.pep.2024.106523

Takahisa Hamano , Makio Yanagisawa , Seiji Hobo

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引用次数: 0

摘要

我们曾在瓶鼻海豚（Tursiops truncatus）中发现表面活性蛋白 D（SP-D）是鲸类肺部免疫系统的独特进化因子。在这篇简短的报告中，我们在哺乳动物细胞中合成了瓶鼻海豚的重组 SP-D（dSP-D），并在体外分析了其特性。使用镍载体或共载体纯化了重组蛋白。十二烷基硫酸钠聚丙烯酰胺凝胶电泳和 Western 印迹显示了一个 50 kDa 的主要条带和次要条带。类似酶联免疫吸附试验的方法显示，重组 dSP-D 与革兰氏阳性和革兰氏阴性细菌的菌壁结合。我们的研究结果表明，dSP-D 可用于鲸目动物肺炎的临床治疗。

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Expression and basic biochemical characteristics of recombinant surfactant protein D of bottlenose dolphin (Tursiops truncatus)

We previously identified surfactant protein D (SP-D) in the bottlenose dolphin Tursiops truncatus as a unique evolutionary factor of the cetacean pulmonary immune system. In this short report, recombinant SP-D of bottlenose dolphin (dSP-D) was synthesized in mammalian cells, and its properties were analyzed in vitro. The recombinant proteins were purified using Ni-carrier or Co-carrier. Sodium dodecyl sulfate poly-acrylamide gel electrophoresis and western blotting revealed a 50 kDa major band with minor secondary bands. Enzyme-linked immunosorbent assay-like methods revealed that recombinant dSP-D bonded to gram-positive and gram-negative bacterial walls. Our findings suggest the clinical usefulness of dSP-D for cetacean pneumonia.

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来源期刊

Protein expression and purification 生物-生化研究方法

CiteScore

3.70

自引率

6.20%

发文量

120

审稿时长

32 days

期刊介绍： Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.