A genetically engineered purpurin/retinol-binding protein hybrid that binds to transthyretin.
A mini-gene encoding rat retinol-binding protein (RBP) and a cDNA encoding chicken purpurin were separately transfected into HeLa cells. In contrast to RBP, expressed purpurin did not bind to transthyretin (TTR). A purpurin/RBP hybrid protein was constructed by substituting the cDNA sequence encoding the N-terminal 29 amino acids of purpurin for the corresponding part of RBP. The expressed hybrid molecule bound to the TTR-Sepharose. These results demonstrate that purpurin does not bind to TTR, that a functional purpurin/RBP hybrid can be constructed, and that the N-terminal coil of RBP is not required for TTR binding.
Melhus
H
H
Department of Cell Research, Uppsala University, Sweden.
Rask
L
L
D000595:Amino Acid Sequence; D000818:Animals; D000880:Anthraquinones; D000911:Antibodies, Monoclonal; D002645:Chickens; D006367:HeLa Cells; D006801:Humans; D037102:Lectins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011228:Prealbumin / Q000378:metabolism*; D015202:Protein Engineering; D051381:Rats; D012177:Retinol-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D014162:Transfection
D000880:Anthraquinones; D000911:Antibodies, Monoclonal; D037102:Lectins; D011228:Prealbumin; D012177:Retinol-Binding Proteins; C511975:purpurin anthraquinone