Abstract
1. 1. Ovine placental lactogen was modified by reaction with o-nitrophenylsulfenyl chloride. Fluorescence measurements indicated that one of the two tryptophan residues of the molecule had reacted. Besides, there was some reagent not covalently bound. 2. 2. The reagent was covalently bound to Trp-150. No evidence of modification of Trp-90 was found. 3. 3. Binding capacity to lactogenic as well as somatogenic receptors was diminished but not abolished upon modification, indicating that absolute molecular integrity of Trp-150 is not required for binding. 4. 4. This behavior is similar to that of the tryptophan residues of ovine prolactin.
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