Different effects of L-arginine on protein refolding: suppressing aggregates of hydrophobic interaction, not covalent binding.

Chen, Jing

Different effects of L-arginine on protein refolding: suppressing aggregates of hydrophobic interaction, not covalent binding. [electronic resource] - Biotechnology progress - 1365-72 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

1520-6033

10.1002/btpr.93 doi


Animals
Arginine--chemistry
Binding Sites
Carbonic Anhydrase I--chemistry
Cattle
Dose-Response Relationship, Drug
Electrophoresis, Polyacrylamide Gel
Granulocyte Colony-Stimulating Factor--chemistry
Green Fluorescent Proteins--chemistry
Humans
Hydrophobic and Hydrophilic Interactions
Kinetics
Protein Folding--drug effects
Recombinant Proteins--chemistry