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G. D., De Robertis, E. D. P.: Cholinergic and non-cholinergic nerve endings in the rat brain. II. Subcellular localization of monoamine oxidase and succinic dehydrogenase. J. Neurochem. 9, 503–508 (1962).",{"doi":501},"10.1111\u002Fj.1471-4159.1962.tb04203.x",{"id":18,"text":503,"url":18,"identifiers":504},"Basolo, F., Johnson, R. C.: Coordination chemistry. New York-Amsterdam: W. A. Benjamin, Inc. 1964.",{},{"id":18,"text":506,"url":18,"identifiers":507},"Bloom, F. E.: The fine structural localization of biogenic amines in nervous tissue. Int. Rev. Neurobiol. 13, 27 (1970).",{"doi":508},"10.1016\u002FS0074-7742(08)60165-8",{"id":18,"text":510,"url":18,"identifiers":511},"Bloom, F. E., Sims, K. L., Weitsen, H. A., David, G. A., Hanker, J. S.: Cytochemical differentiation between monoamine oxidase and other neuronal oxidases. In: Monoamine oxidases: New Vistas. (E. Costa, G. L. Gessa, G. Pepeu and M. Sandler, eds.). New York: Raven Press (in press).",{},{"id":18,"text":513,"url":18,"identifiers":514},"Boadle, M. C., Bloom, F. E.: A method for the fine structural localization of monoamine oxidase. J. Histochem. Cytochem. 17, 331–340 (1969).",{"doi":515},"10.1177\u002F17.5.331",{"id":18,"text":517,"url":18,"identifiers":518},"Cowie, J. M. G., Toporowski, P. M.: Association in the binary liquid system dimethyl sulfoxide-water. Can. J. Chem. 39, 2240–2243 (1961).",{"doi":519},"10.1139\u002Fv61-296",{"id":18,"text":521,"url":18,"identifiers":522},"de Duve, C.: Principles of tissue fractionation. J. Theor. Biol. 6, 33–59 (1964).",{"doi":523},"10.1016\u002F0022-5193(64)90065-7",{"id":18,"text":525,"url":18,"identifiers":526},"El-Badawi, A., Schenk, E. A.: Histochemical methods for separate, consecutive and simultaneous demonstration of acetylcholinesterase and norepinephrine in cryostat sections. J. Histochem. Cytochem. 15, 580–588 (1967).",{"doi":527},"10.1177\u002F15.10.580",{"id":18,"text":529,"url":18,"identifiers":530},"Fahimi, H. D., Amarasingham, C. R.: Cytochemical localization of lactic dehydrogenase in white skeletal muscle. J. Cell Biol. 22, 29–48 (1964).",{"doi":531},"10.1083\u002Fjcb.22.1.29",{"id":18,"text":533,"url":18,"identifiers":534},"Friede, R. L.: Topographic brain chemistry. New York and London: Academic Press 1966.",{},{"id":18,"text":536,"url":18,"identifiers":537},"George, H., McMahan, J., Bowler, K., Elliott, M.: Stabilization of lactate and malate dehydrogenase by organic solvents. Biochim. biophys. Acta (Amst.) 191, 466–468 (1969).",{"doi":538},"10.1016\u002F0005-2744(69)90266-6",{"id":18,"text":540,"url":18,"identifiers":541},"Giacobini, G., Kerpel-Fronius, S.: Histochemical and biochemical correlations of monoamine oxidase activity in autonomic and sensory ganglia of the cat. Acta physiol. scand. 78, 522–528 (1970).",{"doi":542},"10.1111\u002Fj.1748-1716.1970.tb04688.x",{"id":18,"text":544,"url":18,"identifiers":545},"Glenner, G. G., Burtner, H. J., Brown, G. W., Jr.: The histochemical demonstration of monoamine oxidase activity by tetrazolium salts. J. Histochem. Cytochem. 5, 591–600 (1957).",{"doi":546},"10.1177\u002F5.6.591",{"id":18,"text":548,"url":18,"identifiers":549},"Glenner, G. G., Weissbach, H., Redfield, B. G.: The histochemical demonstration of enzymatic activity by a nonenzymatic redox reaction. Reduction of tetrazolium salts by indole-3-acetaldehyde. J. Histochem. Cytochem. 8, 258–261 (1960).",{"doi":550},"10.1177\u002F8.4.258",{"id":18,"text":552,"url":18,"identifiers":553},"Gorkin, V. Z.: Monoamine oxidase activity in membrane structures of rat liver cell. Experientia (Basel) 27, 30 (1971).",{"doi":554},"10.1007\u002FBF02137723",{"id":18,"text":556,"url":18,"identifiers":557},"Graham, R. C., Jr., Karnovsky, M. J.: The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique. J. Histochem. Cytochem. 14, 291–301 (1966).",{"doi":558},"10.1177\u002F14.4.291",{"id":18,"text":560,"url":18,"identifiers":561},"Hanker, J. S., Anderson, W. A., Bloom, F. E.: Osmiophilic polymer generation: catalysis by transition metal compounds in ultrastructural cytochemistry. Science 175, 991–993 (1972a).",{"doi":562},"10.1126\u002Fscience.175.4025.991",{"id":18,"text":564,"url":18,"identifiers":565},"Hanker, J. S., Kasler, F., Bloom, M. G., Copeland, J. S., Seligman, A. M.: Coordination polymers of osmium; the nature of osmium black. Science 156, 1737–1738 (1967).",{"doi":566},"10.1126\u002Fscience.156.3783.1737",{"id":18,"text":568,"url":18,"identifiers":569},"Hanker, J. S., Kusyk, C. J., Clapp, D. H., Yates, P. J.: Effect of dimethylsulfoxide (DMSO) on the histochemical demonstration of dehydrogenases. J. Histochem. Cytochem. 18, 673 (1970).",{},{"id":18,"text":571,"url":18,"identifiers":572},"Hanker, J. S., Seaman, A. R., Weiss, L. P., Ueno, H., Bergman, R. A., Seligman, A. M.: Osmiophilic reagents; new Cytochemical principle for light and electron microscopy. Science 146, 1039–1043 (1964).",{"doi":573},"10.1126\u002Fscience.146.3647.1039",{"id":18,"text":575,"url":18,"identifiers":576},"Hanker, J. S., Yates, P. E., Clapp, D. H., Anderson, W. A.: New methods for the demonstration of lysosomal hydrolases by the formation of osmium blacks. Histochemie 30, 201–214 (1972b).",{"doi":577},"10.1007\u002FBF00277592",{"id":18,"text":579,"url":18,"identifiers":580},"Haugaard, N., Lee, N. H., Kostrzewa, R., Horn, R. S., Haugaard, E. S.: The role of sulfhydryl groups in oxidative phosphorylation and ion transport by rat liver mitochondria. Biochim. biophys. Acta (Amst.) 172, 198–204 (1969).",{"doi":581},"10.1016\u002F0005-2728(69)90063-2",{"id":18,"text":583,"url":18,"identifiers":584},"Henderson, T. R., Henderson, R. F., Johnson, G. E.: The effect of dimethyl sulfoxide on the allosteric transitions of glutamic dehydrogenase. Arch. Biochem. 132, 242–248 (1969).",{"doi":585},"10.1016\u002F0003-9861(69)90358-0",{"id":18,"text":587,"url":18,"identifiers":588},"Hess, R., Scarpelli, D. G., Pearse, A. G. E.: The Cytochemical localization of oxidative enzymes. II. Pyridine nucleotide-linked dehydrogenases. J. biophys. biochem. Cytol. 4, 753–760 (1958).",{"doi":589},"10.1083\u002Fjcb.4.6.753",{"id":18,"text":591,"url":18,"identifiers":592},"Hultin, H. O., Westort, C.: Factors affecting the distribution of lactic dehydrogenase between particulate and nonparticulate fractions of homogenized skeletal muscle. Arch. Biochem. 117, 523–533 (1966).",{"doi":593},"10.1016\u002F0003-9861(66)90093-2",{"id":18,"text":595,"url":18,"identifiers":596},"Johnson, D., Lardy, H.: Isolation of liver or kidney mitochondria. In: Oxidation and phosphorylation (R. W. Estabrook and M. E. Pullman, eds.), Methods in enzymology, vol. 10, p. 94–96. New York: Academic Press 1967.",{"doi":597},"10.1016\u002F0076-6879(67)10018-9",{"id":18,"text":599,"url":18,"identifiers":600},"Kalina, M., Weavers, B., Pearse, A. G. E.: Fine structural localization of succinoxidase complex on the mitochondrial cristae. Nature (Lond.) 221, 479–480 (1969).",{"doi":601},"10.1038\u002F221479a0",{"id":18,"text":603,"url":18,"identifiers":604},"Karnovsky, M. J.: The localization of cholinesterase activity in rat cardiac muscle by electron microscopy. J. Cell Biol. 23, 217–232 (1964).",{"doi":605},"10.1083\u002Fjcb.23.2.217",{"id":18,"text":607,"url":18,"identifiers":608},"Karnovsky, M. J.: A formaldehyde-glutaraldehyde fixative of high osmolality for use in electron microscopy. J. Cell Biol. 27, 137A-138A (1965).",{},{"id":18,"text":610,"url":18,"identifiers":611},"Karnovsky, M. J., Roots, L.: A “direct-coloring” thiocholine method for cholinesterases. J. Histochem. Cytochem. 12, 219–221 (1964).",{"doi":612},"10.1177\u002F12.3.219",{"id":18,"text":614,"url":18,"identifiers":615},"Kerpel-Fronius, S., Hajós, F.: The use of ferricyanide for the light and electron microscopic demonstration of succinic dehydrogenase activity. Histochemie 14, 343–351 (1968).",{"doi":616},"10.1007\u002FBF00304258",{"id":18,"text":618,"url":18,"identifiers":619},"Lukaszyk, A.: A method for histochemical demonstration of α-glycerophosphate-ferricyanide oxidoreductase activity. Folia histochem. cytochem. 9, 167–186 (1971).",{},{"id":18,"text":621,"url":18,"identifiers":622},"Mahler, H. R., Cordes, E. H.: Biological chemistry, 2nd ed. New York: Harper & Row 1971.",{},{"id":18,"text":624,"url":18,"identifiers":625},"Manocha, S. L., Bourne, G. H.: Histochemical mapping of monoamine oxidase and lactic dehydrogenase in the pons and mesencephalon of squirrel monkey (Saimiri sciureus). J. Neurochem. 13, 1047–1056 (1966).",{"doi":626},"10.1111\u002Fj.1471-4159.1966.tb04264.x",{"id":18,"text":628,"url":18,"identifiers":629},"Manocha, S. L., Bourne, G. H.: Histochemical mapping of lactate dehydrogenase and monoamine oxidase in the medulla oblongata and cerebellum of squirrel monkey (Saimiri sciureus). J. Neurochem. 15, 1033–1040 (1968).",{"doi":630},"10.1111\u002Fj.1471-4159.1968.tb11646.x",{"id":18,"text":632,"url":18,"identifiers":633},"Manocha, S. L., Shanta, T. R.: Macaca mulatta: Enzyme histochemistry of the nervous system. New York and London: Academic Press 1970.",{},{"id":18,"text":635,"url":18,"identifiers":636},"Mattison, A. G. M., Johannson, R. G., Bostrom, S.-L.: The cellular localization of lactic dehydrogenase in skeletal muscle of eel (Anguilla anguilla). Comp. Biochem. Physiol. 41B, 475–482 (1972).",{},{"id":18,"text":638,"url":18,"identifiers":639},"McLaughlin, J. A.: Electron donors in tissues. Proc. nat. Acad. Sci. (Wash.) 60, 1418–1419 (1968).",{"doi":640},"10.1073\u002Fpnas.60.4.1418",{"id":18,"text":642,"url":18,"identifiers":643},"Misch, D. W., Misch, M. S.: Dimethylsulfoxide: activation of lysosomes in vitro. Proc. nat. Acad. Sci. (Wash.) 58, 2462–2467 (1967).",{"doi":644},"10.1073\u002Fpnas.58.6.2462",{"id":18,"text":646,"url":18,"identifiers":647},"Misch, D. W., Misch, M. S.: Reversible activation of lysosomes in dimethyl sulfoxide. Nature (Lond.) 221, 862–863 (1969).",{"doi":648},"10.1038\u002F221862a0",{"id":18,"text":650,"url":18,"identifiers":651},"Nara, S., Yasunobu, K. T.: Some recent advances in the field of amine oxidases. In: The biochemistry of copper (J. Peisach, P. Aisen, W. Blumberg, eds.), p. 423–441. New York-London: Academic Press 1966.",{},{"id":18,"text":653,"url":18,"identifiers":654},"Ogawa, K., Saito, T., Mayahara, H.: The site of ferricyanide reduction by reductases within mitochondria as studied by electron microscopy. J. Histochem. Cytochem. 16, 49–57 (1968).",{"doi":655},"10.1177\u002F16.1.49",{"id":18,"text":657,"url":18,"identifiers":658},"Pearse, A. G. E.: Histochemistry, theoretical and applied. Boston: Little, Brown & Co. 1961",{},{"id":18,"text":660,"url":18,"identifiers":661},"Pearse, A. G. E.: Histochemistry, theoretical and applied, vol 1, 3rd ed. Boston: Little Brown & Co. 1968.",{},{"id":18,"text":663,"url":18,"identifiers":664},"Pearse, A. G. E., Scarpelli, D. G.: Intramitochondrial localization of oxidative enzyme systems. Exp. Cell Res., Suppl. 7, 50–64 (1959).",{"doi":665},"10.1016\u002F0014-4827(59)90234-4",{"id":18,"text":667,"url":18,"identifiers":668},"Rammler, D. H., Zaffaroni, A.: Biological implications of DMSO based on a review of its chemical properties. Ann. N.Y. Acad. Sci. 141, 13–23 (1967).",{"doi":669},"10.1111\u002Fj.1749-6632.1967.tb34861.x",{"id":18,"text":671,"url":18,"identifiers":672},"Reid, E.: Biochemical approaches to cancer. Oxford: Pergamon Press Ltd. 1965.",{},{"id":18,"text":674,"url":18,"identifiers":675},"Reiss, J.: Dimethylsulfoxide as carrier in enzyme cytochemistry. Histochemie 26, 93–94 (1971).",{"doi":676},"10.1007\u002FBF00307789",{"id":18,"text":678,"url":18,"identifiers":679},"Samorajski, T.: The application of diphosphoridine nucleotide diaphorase methods in a study of dorsal ganglia and spinal cord. J. Neurochem. 5, 349–353 (1960).",{"doi":680},"10.1111\u002Fj.1471-4159.1960.tb13373.x",{"id":18,"text":682,"url":18,"identifiers":683},"Schneider, W. C.: Enzymatic activities of subcellular fractions. In: Handbook of biochemistry (H. A. Sober, ed.), p. K3-K13. Cleveland: Chemical Rubber Co. 1968.",{},{"id":18,"text":685,"url":18,"identifiers":686},"Seligman, A. M., Karnovsky, M. J., Wasserkrug, H. L., Hanker, J. S.: Nondroplet ultrastructural demonstration of cytochrome oxidase activity with a polymerizing osmiophilic reagent, diaminobenzidine (DAB). J. 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G.: Preparation of nonfrozen sections for electron microscope cytochemistry. Scient. Instr. News., R. C. A. 10, 12–17 (1965).",{},{"id":18,"text":703,"url":18,"identifiers":704},"Szent-Györgi, A.: Charge transfer and electronic mobility. Proc. nat. Acad. Sci. (Wash.) 58, 2012–2014 (1967).",{"doi":705},"10.1073\u002Fpnas.58.5.2012",{"id":18,"text":707,"url":18,"identifiers":708},"Tewari, H. B., Bourne, G. H.: Histochemical studies on the distribution of monoamine oxidase in the cerebellum of rat. Acta anat. (Basel) 52, 334–340 (1963).",{"doi":709},"10.1159\u002F000142368",{"id":18,"text":711,"url":18,"identifiers":712},"Thomas, E., Pearse, A. G. E.: The fine localization of dehydrogenases in the nervous system. Histochemie 2, 266–282 (1961).",{"doi":713},"10.1007\u002FBF00736504",{"id":18,"text":715,"url":18,"identifiers":716},"Tsou, K. C., Goodwin, C. 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