期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 47, 期 1, 页码 281-288出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2005.10.018
关键词
transgenic protein expression; In vivo electroporation; fluorescent proteins; gene expression; mammalian skeletal muscle
类别
资金
- NIAMS NIH HHS [AR47664, AR25201] Funding Source: Medline
The production of mammalian proteins in sufficient quantity and quality for structural and functional studies is a major challenge in biology. Intrinsic limitations of yeast and bacterial expression systems preclude their use for the synthesis of a significant number of mammalian proteins. This creates the necessity of well-identified expression systems based on mammalian cells. In this paper, we demonstrate that adult mammalian skeletal muscle, transfected in vivo by electroporation with DNA plasmids, is an excellent heterologous mammalian protein expression system. By using the fluorescent protein EGFP as a model, it is shown that muscle fibers express, during the course of a few days, large amounts of authentic replicas of transgenic proteins. Yields of similar to 1 mg/g of tissue were obtained, comparable to those of other expression systems. The involvement of adult mammlian cells assures an optimal environment for proper protein folding and processing. All these advantages complement a methodology that is universally accessible to biomedical investigators and simple to implement. (c) 2005 Elsevier Inc. All rights reserved.
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