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Biotechnology Letters 25: 213–218, 2003. 213
© 2003 Kluwer Academic Publishers. Printed in the Netherlands.
High expression of a human lactoferrin in transgenic tobacco cell cultures
1 1 2 2 3
Sun-Mee Choi , Ok-Sun Lee , Suk-Yoon Kwon , Sang-Soo Kwak , Dae-Yeul Yu Haeng-
Soon Lee1,∗
Laboratories of 1Plant Cell Biotechnology, 2Environmental Biotechnology and 3Development and Differentiation,
Korea Research Institute of Bioscience and Biotechnology (KRIBB), Oun-Dong 52, Yusong, Daejeon 305-806,
Korea
∗Author for correspondence (Fax: +82-42-860-4608; E-mail: hslee@kribb.re.kr)
Received 6 November 2002; Accepted 22 November 2002
Key words: high expression promoter, human lactoferrin, recombinant protein, transgenic plant cell culture
Abstract
Transgenic Nicotiana tabacum cell lines were developed expressing the human lactoferrin gene driven by the
oxidative stress-inducible peroxidase (SWPA2) promoter. Western blot analysis showed the accumulation of both
the full-length human lactoferrin protein as well as a immuno-reactive truncated fragment. Accumulation of human
lactoferrin as monitored by ELISA increased proportionally to cell growth and reached a maximal (up to 4.3% of
total soluble proteins) at the stationary phase of growth. Protein extracts from transgenic tobacco cells exhibited
antibacterial activity.
Introduction plant cell suspension cultures is that recombinant pro-
teins can be produced under certified conditions with
Lactoferrin is an iron-binding glycoprotein with an ap- large scale-up at low cost, but yields are low compared
proxima
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