The capacity of bovine serum amineoxidase (SAG) to oxidize free amino groups of nonconventional substrates, such as polylysine (up to 50 kDa) and some proteins as lysozyme and ribonuclease A, is described. The oxidation was quantified from the amount of H2O2 and NH3 enzymatically produced by SAG. Kinetic analysis indicated a stereospecific preference for L-configuration. Maximal oxidation rate was obtained with poly-L-lysine (9.6 kDa). After 10 h of incubation at 37 degrees C, the poly-l-lysine was partially oxidized generating 1.5 moles of H2O2 by one mole of polylysine. Denatured SAO presented very low oxidation rates with the mentioned substrates. (C) 1996 Academic Press, Inc.
Extended substrate specificity of serum amine oxidase: Possible involvement in protein posttranslational modification / Xintao, Wang; Pietrangeli, Paola; Mircea Alexandru, Mateescu; Mondovi', Bruno. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 223:1(1996), pp. 91-97. [10.1006/bbrc.1996.0851]
Extended substrate specificity of serum amine oxidase: Possible involvement in protein posttranslational modification
PIETRANGELI, Paola;MONDOVI', Bruno
1996
Abstract
The capacity of bovine serum amineoxidase (SAG) to oxidize free amino groups of nonconventional substrates, such as polylysine (up to 50 kDa) and some proteins as lysozyme and ribonuclease A, is described. The oxidation was quantified from the amount of H2O2 and NH3 enzymatically produced by SAG. Kinetic analysis indicated a stereospecific preference for L-configuration. Maximal oxidation rate was obtained with poly-L-lysine (9.6 kDa). After 10 h of incubation at 37 degrees C, the poly-l-lysine was partially oxidized generating 1.5 moles of H2O2 by one mole of polylysine. Denatured SAO presented very low oxidation rates with the mentioned substrates. (C) 1996 Academic Press, Inc.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
