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Recombinant functional human lactoferrin expressed in baculovirus system.

Tao Liu¹, Yao-Zhou Zhang, Xiang-Fu Wu

¹Institute of Biochemistry, Zhejiang Sci-Tec University, Hangzhou 310018, China.

Acta Biochimica Et Biophysica Sinica

|March 7, 2006

Summary

Researchers developed a novel method to produce biologically active recombinant human lactoferrin (rhLf) using a recombinant virus and BmN cells. This efficient production of rhLf protein opens avenues for future applications.

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Area of Science:

Biotechnology
Molecular Biology
Protein Expression

Background:

Human lactoferrin (hLf) is an iron-binding glycoprotein with diverse biological functions.
Efficient production of hLf is crucial for its therapeutic and industrial applications.

Purpose of the Study:

To establish a method for the efficient production of recombinant human lactoferrin (rhLf).
To characterize the expressed rhLf protein.

Main Methods:

Amplification of hLf cDNA using reverse transcription-polymerase chain reaction.
Construction of a recombinant baculovirus (vBm-hLf) carrying the hLf gene.
Expression of rhLf in BmN insect cells.

Main Results:

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The nucleotide sequence of the amplified hLf cDNA matched the known sequence.

A recombinant protein with an approximate molecular mass of 78 kDa was expressed.

Approximately 13.5 μg of biologically active rhLf was purified from 1-2x10^5 infected BmN cells.

Conclusions:

A novel and efficient method for producing biologically active rhLf has been established.
This method holds promise for the large-scale production of rhLf for future applications.