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. 1977 Mar;9(2):171-81.
doi: 10.1007/BF01003629.

The cytochemical demonstration of catalase and D-amino acid oxidase in the microbodies of teleost kidney cells

Free article

The cytochemical demonstration of catalase and D-amino acid oxidase in the microbodies of teleost kidney cells

M Veenhuis et al. Histochem J. 1977 Mar.
Free article

Abstract

The distribution of catalase and D-amino acid oxidase, marker enzymes for peroxisomes, was determined cytochemically in the kidney tubules of an euryhaline teleost, the three-spined stickleback. Catalase activity was localized with the diaminobenzidine technique. The presence of D-amino acid oxidase was determined using H2O2 generated by the enzyme, D-alanine as a substrate, and cerous ions for the formation of an electron-dense precipitate. Both enzymes appeared to be located in microbodies. The combined presence of these enzymes characterizes the microbodies as peroxisomes. Biochemically and cytochemically, no urate oxidase or glycolate-oxidizing L-alpha-hydroxy acid oxidase could be demonstrated. Stereological analysis of the epithelia lining the renal tubules showed that the fractional volume of the microbodies is 5 to 10 times higher in the cells of the second proximal tubules than in the other nephronic segments or the ureter. The fractional volume of the microbodies was similar in kidneys of freshwater and seawater fishes.

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References

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