Abstract: Oxytocin and vasopressin are oxidized by horseradish peroxidase and by lactoperoxidase, in the presence of hydrogen peroxide. Spectrophotometric measurements are indicative of the formation of dityrosine. Kinetic parameters indicate that the affinity of horseradish peroxidase is slightly higher for oxytocin with respect to vasopressin and that the two hormones are better substrates for both peroxidases than free tyrosine.
The oxidation of oxytocin and vasopressin by the peroxidase/H2O2 system / Rosei, Maria Anna; Coccia, Raffaella; Blarzino, Carla; C., Foppoli; Mosca, Luciana. - In: AMINO ACIDS. - ISSN 0939-4451. - STAMPA. - 8:(1995), pp. 385-391. [10.1007/BF00806556]
The oxidation of oxytocin and vasopressin by the peroxidase/H2O2 system
ROSEI, Maria Anna;COCCIA, Raffaella;BLARZINO, Carla;MOSCA, Luciana
1995
Abstract
Abstract: Oxytocin and vasopressin are oxidized by horseradish peroxidase and by lactoperoxidase, in the presence of hydrogen peroxide. Spectrophotometric measurements are indicative of the formation of dityrosine. Kinetic parameters indicate that the affinity of horseradish peroxidase is slightly higher for oxytocin with respect to vasopressin and that the two hormones are better substrates for both peroxidases than free tyrosine.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
