Basic and acidic hydrophilic residues involved in the interaction between protomers of the bovine growth hormone dimer.
Reactivity of histidine and arginine residues--as well as of carboxyl-groups--in the covalently stabilized dimer of bovine growth hormone, was studied in comparison with their reactivity in the monomeric form. Results obtained by reaction of histidine and arginine residues with ethoxyformic anhydride and cyclohexanedione, respectively, were similar for both proteins. The reactivity of two carboxyl-groups towards a soluble carbodiimide becomes impaired in the dimer, thus suggesting that their location is within the protomer interaction area.
D001120:Arginine / Q000378:metabolism*; D003510:Cyclohexanes / Q000378:metabolism*; D003512:Cyclohexanones / Q000378:metabolism*; D013006:Growth Hormone / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism*; D007700:Kinetics; D013329:Structure-Activity Relationship
D003510:Cyclohexanes; D003512:Cyclohexanones; D006639:Histidine; C018031:1,2-cyclohexanedione; D013006:Growth Hormone; D001120:Arginine