Barbara Manconi, Irene Messana, Federica Maggiani, Alessandra Olianas, Mariagiuseppina Pellegrini, Roberto Crnjar, Massimo Castagnola, Bruno Giardina, Maria Teresa Sanna
Structural analysis of the hemoglobin (Hb) system of Delphinus delphis revealed a high globin multiplicity: HPLC-electrospray ionization-mass spectrometry (ESI-MS) analysis evidenced three major beta (beta1 16,022 Da, beta2 16,036 Da, beta3 16,036 Da, labeled according to their progressive elution times) and two major alpha globins (alpha1 15,345 Da, alpha2 15,329 Da). ESI-tandem mass and nucleotide sequence analyses showed that beta2 globin differs from beta1 for the substitution Val126 --> Leu, while beta3 globin differs from beta2 for the isobaric substitution Lys65 --> Gln...
November 2009: Journal of Comparative Physiology. B, Biochemical, Systemic, and Environmental Physiology