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Structural investigation of tumor differentiation factor
Urmi Roy1, Izabela Sokolowska, Alisa G Woods
1Biochemistry & Proteomics Group, Department of Chemistry & Biomolecular Science, Clarkson University, Potsdam, NY, USA.
Biotechnology and Applied Biochemistry
|April 17, 2013
Summary
Tumor differentiation factor (TDF), a pituitary protein, was studied for its function. Recombinant TDF (rTDF) showed varied expression, while native TDF appeared as a 50 kDa band, suggesting complex disulfide bonding.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Tumor differentiation factor (TDF) is a 17 kDa pituitary protein with unknown function.
- TDF contains four cysteine residues (Cys17, Cys70, Cys97, Cys98) crucial for protein structure and function.
- Incomplete characterization necessitates further investigation into TDF's properties and biological role.
Purpose of the Study:
- To overexpress and characterize recombinant TDF (rTDF).
- To investigate the properties of native, secreted TDF.
- To predict potential disulfide connectivities within TDF using molecular modeling.
Main Methods:
- Recombinant TDF (rTDF) overexpression and characterization.
- Western blotting (WB) for rTDF and native TDF detection.
- Mass spectrometry for rTDF peptide identification.
- Molecular modeling for disulfide bridge prediction.
Main Results:
- rTDF was predominantly expressed as insoluble monomers and dimers.
- Mass spectrometry confirmed the presence of a TDF peptide.
- Native, secreted TDF was detected as a 50 kDa band via WB.
- Molecular modeling suggested potential disulfide bridges between Cys17-Cys98 and Cys70-Cys17.
Conclusions:
- The study provides initial characterization of TDF, including its expression patterns and potential structural features.
- Discrepancies in molecular weight between recombinant and native TDF suggest post-translational modifications or complex folding.
- Predicted disulfide bridges offer insights into TDF's tertiary structure and potential function.
