Kinetics of appearance of hemorphins from bovine hemoglobin peptic hydrolysates by a direct coupling of reversed-phase high-performance liquid chromatography and electrospray ionization mass spectrometry.
Reversed-phase high-performance liquid chromatography coupled with electrospray ionization mass spectrometry was used to improve the preparation of three opioid peptides (Leu-Val-Val-hemorphin-7, Val-Val-hemorphin-7 and Val-Val-hemorphin-4) resulting from bovine hemoglobin peptic hydrolysates. Optimal conditions for the preparation of these peptides were determined thanks to their kinetic studies of appearance in the course of peptic hydrolyses as a function of degree of hydrolysis of hemoglobin. We propose a low degree of hydrolysis (3%) to prepare Leu-Val-Val-hemorphin-7, a mean degree of hydrolysis (11%) to prepare Val-Val-hemorphin-7 and a high degree of hydrolysis (21%) to prepare Val-Val-hemorphin-4.
Froidevaux
R
R
Laboratoire de Technologie des Substances Naturelles, IUT A Lille 1, Villeneuve d'Ascq, France.
Lignot
B
B
Nedjar-Arroume
N
N
Guillochon
D
D
Coddeville
B
B
Ricart
G
G
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D006454:Hemoglobins / Q000737:chemistry*; D006868:Hydrolysis; D007700:Kinetics; D013058:Mass Spectrometry / Q000379:methods*; D018847:Opioid Peptides / Q000737:chemistry*
D006454:Hemoglobins; D018847:Opioid Peptides