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Detection and characterization by high‐performance liquid chromatography and mass spectrometry of two truncated goat α s 2 ‐caseins
Author(s) -
Cunsolo Vincenzo,
Muccilli Vera,
Saletti Rosaria,
Marletta Donata,
Foti Salvatore
Publication year - 2006
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.2415
Subject(s) - chemistry , mass spectrometry , chromatography , protein mass spectrometry , electrospray ionization , high performance liquid chromatography , tandem mass spectrometry , trypsin , sample preparation in mass spectrometry , electrospray , analytical chemistry (journal) , biochemistry , enzyme
Abstract The identification and characterization of truncated forms of goat α s 2 ‐Cn variants A and E are reported. The two proteins, which have experimental M r values of 24 183 and 24 227 Da, were detected as minor components in a goat milk sample from an autochthonous breed of southern Italy, ‘Rossa Mediterranea’, by reversed‐phase high‐performance liquid chromatography/electrospray ionization mass spectrometry (RP‐HPLC/ESI‐MS). Characterization of the amino acid sequences, performed by coupling trypsin digestion with matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS), RP‐HPLC/ESI‐MS and tandem mass spectrometry (MS/MS), demonstrated that the polypeptide chains correspond to the 1‐204 sequence of mature α s 2 ‐Cn variant A (component with M r of 24 183 Da) and E (component with M r of 24 227 Da), respectively. These components seem to be the product of a differential splicing of pre‐messenger RNA during the translation process of the α s 2 ‐Cn variants A and E. Copyright © 2006 John Wiley & Sons, Ltd.