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Author(s): Nipunjot Kaur Soni-Bains1* and Praveen Pal Balgir 2

The fission yeast Schizosaccharomyces pombe, is an attractive host modelfor high-level protein production and functional analysis of eukaryotic proteins as it shares many molecular, genetic and biochemical features with higher eukaryotes such as plants and animals. Furthermore, S. pombe has a developed Golgi apparatus and galactosyltransferase that is not found in other yeast cells. Moreover many types of human proteins have been successfully expressed in S. pombe, and it has also been used effectively for production of many types of heterologous proteins. However, one of the major hurdles in efficient production and purification of heterologous proteins from S. pombeis proteolytic degradation of the recombinant gene products by host-specific proteases. The problem becomes significant when the recombinant protein under production, is secretory and proteolytically sensitive in nature. Present study aims at controlling the protease activity by gene silencing approach. A Protease silencing cassette was designed to impede the protease enzyme post trascriptionally. Since all proteases do not attack all proteins, only protein specific protease is sought to be silenced as a test case in this study.

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pharmaceutical analysis, international journal, chemical and pharmaceutical, journal of chemical, online open access journals, open access journals
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Citations : 440

International Journal of Chemical and Pharmaceutical Analysis received 440 citations as per google scholar report

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