TY - JOUR
T1 - Extended substrate specificity of serum amine oxidase
T2 - Possible involvement in protein posttranslational modification
AU - Wang, Xintao
AU - Pietrangeli, Paola
AU - Mateescu, Mircea Alexandru
AU - Mondovi, Bruno
N1 - Funding Information:
This work was supported by a joint MRC (Canada) - CNR (Italy) research agreement (M.A.M. and B.M.) and by grants from CNR project on “Biotecnologie e Biologia Molecolare” and from MURST (Italy).
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1996/6/5
Y1 - 1996/6/5
N2 - 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°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.
AB - 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°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.
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U2 - 10.1006/bbrc.1996.0851
DO - 10.1006/bbrc.1996.0851
M3 - Article
C2 - 8660385
AN - SCOPUS:0029982707
SN - 0006-291X
VL - 223
SP - 91
EP - 97
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -