scholarly journals Methylamine and benzylamine induced hypophagia in mice: Modulation by semicarbazide-sensitive benzylamine oxidase inhibitors and aODN towards Kv1.1 channels

2001 ◽  
Vol 134 (4) ◽  
pp. 880-886 ◽  
Author(s):  
R Pirisino ◽  
C Ghelardini ◽  
G Banchelli ◽  
N Galeotti ◽  
L Raimondi
Keyword(s):  
Benzylamine Oxidase

BENZYLAMINE OXIDASE

The Lancet ◽  
1978 ◽  
Vol 311 (8062) ◽  
pp. 483 ◽  
Keyword(s):  
Benzylamine Oxidase

scholarly journals Comparative studies on benzylamine oxidase in rat stomach, spleen and testis.

1983 ◽  
Vol 33 ◽  
pp. 216
Author(s):  
Hirohisa Tajima ◽  
Hiroyasu Kinemuchi ◽  
Kazuya Kamijo
Keyword(s):  
Comparative Studies ◽  
Rat Stomach ◽  
Benzylamine Oxidase

scholarly journals Steady-State Kinetic Studies on Benzylamine Oxidase from Pig Plasma

2005 ◽  
Vol 114 (1) ◽  
pp. 133-138 ◽  
Author(s):  
Iain D. KELLY ◽  
Peter F. KNOWLES ◽  
Kapil D. S. YADAV ◽  
William G. BARDSLEY ◽  
Paul LEFF ◽  
...  
Keyword(s):  
Steady State ◽  
Kinetic Studies ◽  
Steady State Kinetic ◽  
Benzylamine Oxidase ◽  
State Kinetic

Age-related changes in benzylamine oxidase activity in rat tissues

1984 ◽  
Vol 36 (9) ◽  
pp. 592-596 ◽  
Author(s):  
HUNG CAO DANH ◽  
MARGHERITA STROLIN BENEDETTI ◽  
PHILIPPE DOSTERT ◽  
ARLETTE MOUSSET
Keyword(s):  
Oxidase Activity ◽  
Rat Tissues ◽  
Age Related ◽  
Benzylamine Oxidase ◽  
Age Related Changes

scholarly journals Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods

1979 ◽  
Vol 177 (1) ◽  
pp. 289-302 ◽  
Author(s):  
R Barker ◽  
N Boden ◽  
G Cayley ◽  
S C Charlton ◽  
R Henson ◽  
...  
Keyword(s):  
Magnetic Resonance ◽  
Water Molecule ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Analytical Ultracentrifugation ◽  
The Other ◽  
Water Molecules ◽  
Fast Exchange ◽  
Benzylamine Oxidase ◽  
O2 Binding

Benzylamine oxidase from pig plasma has been studied by a variety of chemical and physical techniques. 1. Analytical ultracentrifugation, gel electrophoresis and isoelectric-focusing studies suggest that the enzyme is composed of two subunits with closely similar primary structures. 2. E.s.r. and n.m.r. measurements show that the enzyme contains two well-separated (greater than 0.6 nm) Cu2+ ions at chemically distinct sites. Each Cu2+ ion is coordinated by two water molecules, one ‘axial’ and the other ‘equatorial’. Both water molecules undergo fast exchange (10(5)–10(8) s-1) with solvent and are deprotonated in the pH r!ange 8–9, but only the equatorial water molecule is displaced by the inhibitors N3- and CN-. 3. Kinetic and e.s.r. measurements show that azide and cyanide compete against O2 binding and also make the two Cu2+ sites identical. It is concluded that Cu2+ must participate in the re-oxidation of reduced enzyme by molecular O2.

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