The reaction of the histidine residues of luteinizing hormone with ethoxyformyl anhydride.
Bovine and porcine luteinizing hormones (B-LH, P-LH) and their subunits were treated by ethoxyformyl anhydride. The acylation of the histidine residues was followed by examination of the absorbance spectrum. All the histidine residues of the luteinizing hormone molecule can be modified at pH5. However 2 His in B-LH and 1 in P-LH appear to be much less reactive at pH 5 than the others and their acylated imidazols more labile at the same pH. At neutral pH, 2 histidines in B-LH (and 1 in P-LH) become unreactive. In the case of the subunits, 1 histidine becomes unreactive in each subunit at neutral pH. These unreactive histidine residues at neutral pH are probably those which appear to be poorly reactive at pH 5. Comparison of the results obtained with B-LH and P-LH suggests that of the 2 histidine residues present in B-LH and absent in P-LH (beta 60, beta 112), only one exhibits a low reactivity. Acylation of 4 His in B-LH do not cause dissociation into subunits of the molecule but supress 95 per cent of the biological activity.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004047:Diethyl Pyrocarbonate; D006639:Histidine / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007986:Luteinizing Hormone; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity; D013552:Swine
D006639:Histidine; D007986:Luteinizing Hormone; D004047:Diethyl Pyrocarbonate