Purification and characterization of recombinant osteocalcin fusion protein expressed in Escherichia coli.

@article{Kknen1996PurificationAC,
  title={Purification and characterization of recombinant osteocalcin fusion protein expressed in Escherichia coli.},
  author={Sanna M K{\"a}k{\"o}nen and Jukka Hellman and Kim Pettersson and Timo L{\"o}vgren and Matti Karp},
  journal={Protein expression and purification},
  year={1996},
  volume={8 2},
  pages={137-44}
}
Human osteocalcin (hOC) is a 49-amino-acid peptide produced mainly by bone osteoblasts. The amount of hOC in the circulation reflects the status of bone metabolism and it is used to monitor various bone-related diseases. The aim of this study was to produce recombinant human osteocalcin (rhOC) in Escherichia coli and use it for designing new osteocalcin fluorescence immunoassays. Recombinant DNA technology was used to fuse synthetic hOC coding sequences to an affinity handle system based on… CONTINUE READING