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Literature summary extracted from

  • Lee, D.H.; Kim, S.G.; Kweon, D.H.; Seo, J.H.
    Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins (2009), BMC Biotechnol., 9, 27.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.18 expression in Escherichia coli Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.6.1.18 refolding of denatured and reduced RNase A with refolding-facilitating media immobilized with three folding machineries, mini-chaperone (a monomeric apical domain consisting of residues 191-345 of GroEL) and two foldases (DsbA and human peptidyl-prolyl cis-trans isomerase) by mimicking oxidative refolding chromatography. For efficient and simple purification and immobilization simultaneously, folding machineries are fused with the positively-charged consecutive 10-arginine tag at their C-terminal. The immobilized folding machineries are fully functional when assayed in a batch mode Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.18 pancreas
-
 Bos taurus
-

Synonyms

EC Number Synonyms Comment Organism
4.6.1.18 ribonuclease A
-
 Bos taurus
4.6.1.18 RNase A
-
 Bos taurus