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Structural investigation of tumor differentiation factor
Author(s) -
Roy Urmi,
Sokolowska Izabela,
Woods Alisa G.,
Darie Costel C.
Publication year - 2012
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1046
Subject(s) - factor (programming language) , biology , chemistry , computational biology , computer science , programming language
Abstract Tumor differentiation factor ( TDF ) is a 17 kDa protein produced by the pituitary and secreted into the bloodstream, with no definitive function and incomplete characterization. TDF has the following four cysteine ( C ys) residues: C ys17, C ys70, C ys97, and C ys98. To understand the function of TDF , we (1) overexpressed and characterized recombinant TDF (r TDF ); (2) investigated native, secreted TDF ; and (3) assessed potential disulfide connectivities using molecular modeling. Our results from W estern blotting ( WB ) experiments suggest that r TDF is mostly expressed as insoluble, monomeric, and dimeric forms. Mass spectrometry analysis of the overexpressed r TDF identified a peptide that is a part of TDF protein. WB of the native, secreted TDF detected it as a 50 kDa band. In addition, investigation of TDF by molecular modeling suggests that the C ys residues may form disulfide bridges between C ys17– C ys98 and C ys70– C ys17.