1. The accurate molecular weight of the globin chains from river buffalo hemoglobin components has been determined by means of electrospray mass spectrometry. 2. The ES/MS analysis demonstrated that all the buffalo Hb components share a common beta chain whose mass value coincides with that expected on the basis of the reported sequence. 3. The AA phenotype alpha 1 and alpha 3 globin chains exhibited a 30 Da mass difference as compared to their predicted molecular weights. Careful re-examination of the two alpha globin sequences by FAB/MS revealed the occurrence of sequence errors and hence the correct primary structure of both alpha chains was established.