Oxidation of methionine residues in lutropin

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Abstract
Bovine lutropin and its subunits were submitted to oxidation by sodium periodate or chloramine T. Methionine residues were easily oxidized but partial destruction of fucose was observed. After oxidation treatment most of the lutropin exhibits the same elution volume in gel filtration as the native hormone. Sucrose gradient sedimentation or gel filtration experiments show however that the oxidation of isolated subunits is accompanied by aggregation or conformational changes even in the case of porcine β subunit which contains only one methionine residue. Oxidized bovine lutropin was inactive. The recombination product of oxidized porcine β subunit and intact α subunit exhibit very low residual activity.

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