The oxidation of oxytocin and vasopressin by peroxidase/H2O2 system |
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| Authors: | M. A. Rosei R. Coccia C. Blarzino C. Foppoli L. Mosca |
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| Affiliation: | (1) Dipartimento di Scienze Biochimiche !["ldquo"]("/content/v043w53161594237/xlarge8220.gif") A. Rossi Fanelli!["rdquo"]("/content/v043w53161594237/xlarge8221.gif") , Università La Sapienza, P.le A. Moro, 5, I-00185 Roma, Italy;(2) Centro di Biologia Molecolare del C.N.R., P.le A. Moro, 5, I-00185 Roma, Italy |
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| Abstract: | ![]()
Summary 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. |
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| Keywords: | Amino acids Oxytocin Vasopressin Peroxidase Dityrosine |
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