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   <subfield code="a">Enzyme cytochemical localization of sarcosine oxidase activity in the liver and kidney of several mammals</subfield>
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   <subfield code="c">[Miki Chikayama, Mariko Ohsumi, Sadaki Yokota]</subfield>
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   <subfield code="a">Abstract.: We investigated the enzyme cytochemical localization of sarcosine oxidase (SOX) in the liver and kidney of several mammals using a cerium technique. First we measured the enzyme activities in the liver and kidney of several mammals and in several organs of mice. The highest activity was found in the Chinese hamster, followed by the mouse. Therefore, we used hamster and mouse tissues for enzyme cytochemistry. The liver and kidneys were fixed by perfusion with various concentrations of glutaraldehyde for 10min. Tissue slices were incubated in reaction medium consisting of 50mM TRIS-maleate buffer (pH7.8), 9mM sodium azide, 9.8mM sarcosine, 25µM FAD, 2mM cerium chloride, 0.002% saponin, and 0.003% Triton X-100 for 0.5-8h at 37°C. Optimum staining reaction was obtained in tissues fixed with 0.2% glutaraldehyde, followed by incubation for 2-4h. Electron-dense reaction products were present exclusively in peroxisomes. Within the peroxisomes strong reactions were observed in the matrix subjacent to the limiting membrane decreasing toward the center. The staining reaction was completely inhibited by 2mM N-bromosuccinimide. These results indicated that SOX is a peroxisomal enzyme and that the enzyme might be associated with the peroxisomal membrane.</subfield>
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   <subfield code="a">Enzyme cytochemistry Sarcosine oxidase Peroxisomes</subfield>
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   <subfield code="a">Chikayama</subfield>
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   <subfield code="u">Department of Bioscience, Faculty of Science and Engineering, Teikyo University of Science and Technology, 2525 Uenohara, Yamanashi, 409-0193 Japan</subfield>
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