Spectral Studies on Monoamine Oxidase Modified with N-(1-Pyrene) Malemide Fluorescent Probe
Monoamine oxidase is involved in the control of the biogenic amines degradation in the brain and central nervous system (Singer et al., 1979; Usdin, 1976). This involvement has stimulated considerable interest in the physiocochemical and enzymatic properties of the enzyme. The enzyme contains four sulfhydryl groups per subunit of enzyme only one of which is thought to be essential (Oi et al., 1971). Physiochemical studies have indicated that the enzyme is made up of two identical subunits (Igaue et al., 1969). From the effect of pH on the kinetic properties of the enyzme, it was concluded that a cysteine residue in the enzyme is catalytically important in the breakdown of amines. Gomes et al. (1969) have shown that 5,5’dithiobis 2-nitrobenzoic acid (DTNB) reacts with several cysteine residues and causes inactivation of the enzyme, however, the study concluded that only one sulfhydryl residue was essential per subunit of the enzyme. It was suggested that this sulfhydryl residue may be a component of the active site. As a first step toward a three-dimensional model of bovine liver monoamine oxidase-B, Zeidan et al. (1980) embarked upon a specific study of the environment of the sulfhydryl residue using conventional ESR spin-labeling techniques. The details of this aspect of MAO research have been elaborated elsewhere (Zeidan et al., 1980).
KeywordsElectron Paramagnetic Resonance Emission Spectrum Cysteine Residue Monoamine Oxidase Sulfhydryl Group
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