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.
Electrospray mass spectrometric analysis of river buffalo (Bubalus bubalis) hemoglobins. Re-examination of alpha 1 and alpha 3 globin chain sequences / Ferranti, Pasquale; Di Luccia, A; Malorni, A; Ferrara, L; Marino, Gennaro; Pucci, Pietro. - In: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. B, COMPARATIVE BIOCHEMISTRY. - ISSN 0305-0491. - STAMPA. - 105:3-4(1993), pp. 573-578.
Electrospray mass spectrometric analysis of river buffalo (Bubalus bubalis) hemoglobins. Re-examination of alpha 1 and alpha 3 globin chain sequences.
FERRANTI, PASQUALE;MARINO, GENNARO;PUCCI, PIETRO
1993
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
