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THE ULTRASTRUCTURAL LOCALIZATION OF MONOAMINE OXIDASE (MAO) WITH TRYPTAMINE AND A NEW TETRAZOLIUM SALT, 2-(2'-BENZOTHIAZOLYL)-5-STYRYL-3-(4'-PHTHALHYDRAZIDYL) TETRAZOLIUM CHLORIDE (BSPT)

W. ALLEN SHANNON JR. 1, HANNAH L. WASSERKRUG 1, and ARNOLD M. SELIGMAN 1

1 Department of Research Oncology and Cell Biology, Sinai Hospital of Baltimore, Inc., Baltimore, Maryland 21215, and Department of Surgery, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

The ultrastructural localization of monoamine oxidase (MAO) is demonstrated with tryptamine and a new nonosmiophilic tetrazolium salt, 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazidyl) tetrazolium chloride (BSPT), which is reduced to an osmiophilic formazan. Under the cytochemical conditions for conducting osmication, the styryl group is not osmicated. MAO is localized in guinea pig myocardial, renal and hepatic tissues and rat myocardium. Enzymatic activity is demonstrated in endoplasmic reticulum, nuclear envelope and mitochondrial outer compartment, specifically in the outer membrane. Sensitivity to formaldehyde fixation and specific MAO inhibitors indicates that the enzymatic activity is due to MAO and possibly other amine oxidases.

Submitted on June 4, 1973


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Y.-H. Huang, A. Ito, and R. Arai
Immunohistochemical Localization of Monoamine Oxidase Type B in Pancreatic Islets of the Rat
J. Histochem. Cytochem., September 1, 2005; 53(9): 1149 - 1158.
[Abstract] [Full Text] [PDF]



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