Identification and release kinetics of peptides from the process of peptic hydrolysis of bovine hemoglobin by LC-ESI-MS/MS.
Prep Biochem Biotechnol
; 37(2): 123-38, 2007.
Article
en En
| MEDLINE
| ID: mdl-17454823
Bovine hemoglobin was hydrolyzed with pepsin in a batch stirred tank reactor; the resulting peptides were identified, in a time dependent and comprehensive manner, using reversed phase-high performance liquid chromatography (RP-HPLC) coupled with electrospray ionization tandem mass spectrometry (ESI-MS/MS) by means of database searching. Peptic digestion of bovine hemoglobin yields more hydrophobic peptides at a low degree of hydrolysis, and more hydrophilic peptides at a later stage of hydrolysis. The release kinetics of the bioactive peptides was also followed based on the RP-HPLC profiles. In addition, the behavior of peptic digestion of hemoglobin alpha and beta chains was compared in terms of profiling the identified peptides. Thirty-two peptides were recovered by a process of hydrolysis from the alpha chain of the peptide; whereas the corresponding result for the beta chain was 19 peptides with around 67% sequence coverage. The main factor responsible for non-peptic susceptibility of the central region of the beta chain was their relatively higher hydrophilicity.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Hemoglobinas
/
Cromatografía Liquida
/
Espectrometría de Masa por Ionización de Electrospray
Tipo de estudio:
Diagnostic_studies
/
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Prep Biochem Biotechnol
Asunto de la revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
2007
Tipo del documento:
Article
Pais de publicación:
Reino Unido