Journal Article

Recombinant Functional Human Lactoferrin Expressed in Baculovirus System

Tao Liu, Yao-Zhou Zhang and Xiang-Fu Wu

Edited by Zhi-Fang Zhang

in Acta Biochimica et Biophysica Sinica

Published on behalf of Institute of Biochemistry and Cell Biology, SIBS, CAS

Volume 38, issue 3, pages 201-206
Published in print March 2006 | ISSN: 1672-9145
Published online March 2006 | e-ISSN: 1745-7270 | DOI: http://dx.doi.org/10.1111/j.1745-7270.2006.00143.x
Recombinant Functional Human Lactoferrin Expressed in Baculovirus System

Show Summary Details

Preview

Human lactoferrin (hLf) is a multifunctional iron-binding glycoprotein. In this study, we amplified hLf cDNA by reverse transcription-polymerase chain reaction from normal human mammary gland. The nucleotide sequence of the hLf was identical to the known hLf. We constructed a recombinant virus, vBm-hLf, harboring the hLf gene and exploited the BmN cells as host to produce recombinant human lactoferrin (rhLf). It was found that a recombinant protein with a molecular mass of approximately 78 kDa was expressed. Approximately 13.5 μg rhLf was purified from 1–2 × 105 BmN cells infected by vBm-hLf and the rhLf proved to be biologically active. This method established in our study will pave the way for efficient production of rhLf for further application of this protein in the future.

Keywords: bacteriostatic activity; baculovirus; Bombyx mori; human lactoferrin; reverse transcription-polymerase chain reaction

Journal Article.  0 words. 

Subjects: Biochemistry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.