Role of histidine residues in ovine lutropin: Effects on steroidogenic activity

The modification of histidine residues of ovine pituitary lutropin by rose bengal sensitized photooxidation has been investigated. The destruction of an average of one histidine out of six lead to 90% loss of biological activity as examined by the in vitro steroidogenic response in the rat Leydig cell essay. Further modification of an average 2 - 3 histidine residues reduced the biological activity to less than 1% of the native lutropin. The modified lutropin was incapable of inhibiting the native lutropin induced steroidogenesis. Gel filtration experiments and polyacrylamide disc gel electrophoresis patterns indicated that no dissociation of the molecule into subunits occurred. This is the first report on the essentiality of the histidine residue for the activity of lutropin.